Publications
Citations: https://scholar.google.com/citations?user=O7PY3eAAAAAJ&hl=en
Current stats: citations – 24,744; h index – 84; i10 index -227.
Papers
(This list was last updated on August 7, 2024. It is impractical to update it every
month, so please check PubMed for the latest)
2024
Gurevich, V.V., Gurevich, E.V. Multiple functions of arrestin-1. Reference module in neuroscience and biobehavioral psychology. In press; doi: 10.1016/B978-0-443-1382-1.00051-7 (2024).
Gurevich, V.V., Gurevich, E.V. Phototransduction: inactivation in rods. Reference module in neuroscience and biobehavioral psychology. In press; doi: 10.1016/B978-0-12-374203-2.00187-1 (2024).
Gurevich, V.V., Gurevich, E.V. Phototransduction: inactivation in cones. Reference module in neuroscience and biobehavioral psychology. In press; doi: 10.1016/B978-0-12-374203-2.00190-1 (2024).
Gurevich, V.V., Gurevich, E.V. GPCR-dependent and -independent arrestin signaling. Trends Pharmacol Sci 45 (7), 639-650; doi 10.1016/j.tips.2024.05.007 (2024).
Gurevich, V.V. Arrestins: a small family of multi-functional proteins. Int J Mol Sci 25 (11) 6284; doi 10.3390/ijms25226284 (2024).
Ahmed, M.R., Zheng, C., Dunning, J.L., Ahmed, M.S., Ge, C., Pair, F.S., Gurevich, V.V., Gurevich, E.V. Arrestin-3-assisted activation of JNK3 mediates dopaminergic behavioral sensitization. Cell Rep Med 5 (7), 101623; doi: 10.1016/j.xcrm.2024.101623 (2024).
Zheng, C., Nguyen, K.K., Vishnivetskiy, S.A., Gurevich, V.V., Gurevich, E.V. Arrestin-3 binds parkin and enhances parkin-dependent mitophagy. J Neurochem, in press; doi: 10.1111/jnc.16043 (2024).
2023
Zheng, C., Weinstein, L.D., Nguen, K.K., Grewal, A., Gurevich, E.V., Gurevich, V.V. GPCR binding and JNK activation by arrestin-3 have different structural requirements. Cells 12 (12), 1563; doi: 10.3390/cells12121563 (2023)
Gurevich V.V., Gurevich E.V. Mechanisms of arrestin-mediated signaling. Curr Protoc 3 (6), e821; doi: 10.1002/cpz1.821 (2023).
Vishnivetskiy, S.A. Zhan, X., Gurevich V.V. Expression of untagged arrestins in E. coli and their purification. Curr Protoc 3 (9), e832; doi: 1002/cpz1.832 (2023).
Zhan, X., Kaoud, T.S., Dalby, K.N., Gurevich, E.V., Gurevich V.V. Arrestin-3-dependent activation of c-Jun N-terminal kinases (JNKs). Curr Protoc 3 (9), e839; doi: 10.1002/cpz1.839 (2023).
Gurevich, V.V., Gurevich, E.V. Dynamic nature of proteins is critically important for their function: GPCRs and signal transducers. Appl Magn Reson 1-15; doi: 10.1007/s00723-023-01561-8 (2023).
Gurevich, V.V. Do arrestin oligomers have specific functions? Cell signal (Middlet) 1 (1), 42-46; doi: 10.46439/signaling.1.009 (2023).
Zheng, C., Javitch, J.A., Lambert, N.A., Donthamsetti, P., Gurevich, V.V. In-cell arrestin-receptor interaction assays. Curr Protoc 3 (10), e890; doi 1002/cpz1.890 (202
Vishnivetskiy, S.A., Weinstein, L.D., Zheng, C., Gurevich, E.V., Gurevich, V.V. Functional Role of arrestin-1 residues interacting with unphosphorylated rhodopsin elements. Int J Mol Sci 24 (10), 8903; doi.org/10.3390/ijms24108903; 20944/preprints202304.0476.v1 (2023).
Wess, J, Oteng, A.B., Rivera-Gonzalez, O., Gurevich, E.V., Gurevich, V.V. β-Arrestins: Structure, Function, Physiology, and Pharmacological Perspectives. Pharmacol Rev, in press; doi: 10.1124/pharmrev.121.000302 (2023).
Gurevich V.V. Conformational flexibility underlies the versatility of arrestins. BioEssays, in press; doi: 10.1002/bies.202300085 (2023).
Gurevich V.V. Beta-adrenergic receptors. In Primer on Autonomic Nervous System, 4th edition (Biaggioni, I., Browning, K., Fink, G., Jordan, J., Low, P.A., Paton, J.F.R., eds.), San Diego: Elsevier Inc./Academic Press, 53-55 (2023).
Gurevich V.V., Gurevich E.V. A boost in learning by removing nuclear phosphodiesterases and enhancing nuclear cAMP signaling. Sci Signal 16 (778), eadg9504; doi: 10.1126/scisignal.adg9504 (2023).
Caruso, G., Claus, C., Hamm, H.E., Gurevich, V.V., Bisegna, P., Andreucci, D., DiBenedetto, E., Makino, C. Pepperberg Plot: Modeling Flash Response Saturation in Vertebrate Retinal Rods. Front Mol Neurosci, 15, 1054449; doi: 10.3389/fnmol.20221054449 (2023).
Aydin, Y., Böttke, T., Lam, J.H., Ernicke, S., Fortmann, A., Tretbar, M., Zarzycka, B., Gurevich, V.V., Katritch, V., Coin, I. Structural details of a class B GPCR-arrestin complex revealed by genetically encoded crosslinkers in living cells. Nat Commun 14 (1), 1151; doi 10.1038/s41467-023-36797-2 (2023).
2022
Geva, P., Caruso, G., Klaus, C., Hamm, H.E., Gurevich, V.V., DiBenedetto, E., Makino, C.L. Single photon response reproducibility in retinal rods: effects of cell size and bicarbonate. Front Mol Neurosci 16, 1050545; doi: 10.3389/fnmol.2022.1050545 (2022).
Vishnivetskiy, S.A., Huh, E.K., Karnam, P.C., Oviedo, S., Gurevich, E.V., Gurevich, V.V. The Role of arrestin-1 middle loop in rhodopsin binding. Int J Mol Sci 23 (22), 13887; doi: 10.3390/ijms232213887 (2022).
Perry-Hauser, N.A., Kaoud, T.S., Stoy, H., Zhan, X., Chen, Q., Dalby, K.N., Iverson, T.M., Gurevich, V.V., Gurevich, E.V. Short arrestin-3 derived peptides activate JNK3 in cells. Int J Mol Sci 23 (15), 8679; doi: 10.3390/ijms23158679 (2022).
Asher, W.B., Terry, D.S., Gregorio, G.A., Kahsai, A.W., Borgia, A., Xie, B., Modak, A., Zhu, Y., Jang, W., Govindaraju, A., Huang, L.-Y., Inoue, A., Lambert, N.A., Gurevich, V.V., Shi, L., Lefkowitz, R.J., Blanchard, S.C., Javitch, J.A. GPCR-mediated b-arrestin activation deconvoluted with single-molecule precision. Cell 185 (10), 1661-1675.e16; doi: 10.1016/j.cell.2022.03.042 (2022).
Hsieh, C.-H., Yao, Y., Gurevich, V.V., Chen, J. Arrestin facilitates rhodopsin dephosphorylation in vivo. J Neurosci 42 (17), 3537-3545; doi: 10.1523/JNEUROSCI.0141-22.2022 (2022).
Gurevich V.V., Gurevich E.V. History of arrestins. Ch. 1 (pp. 1-8) in “Arrestin: structure and function in vision and beyond”. Gurevich V.V., ed. Academic Press, ISBN: 978-0-323-85756-7; https://doi.org/10.1016/B978-0-323-85756.00003-0 (2022).
Gurevich V.V., Gurevich E.V. Signaling-biased arrestin-based molecular tools. Ch. 7 (pp. 105-124) in “Arrestin: structure and function in vision and beyond”. Gurevich V.V., ed. Academic Press, ISBN: 978-0-323-85756-7; https://doi.org/10.1016/B978-0-323-85756.00007-8 (2022).
Seyedabadi, M., Gharghabi, M., Gurevich, E.V., Gurevich, V.V. Structural basis of GPCR coupling to distinct transducers: implications for biased signaling. Trends Biochem Sci 47 (7), 570-581;doi: 10.1016/j.tibs.2022.03.009 (2022).
Gurevich V.V. Beta-adrenergic receptors. In Autonomic Nervous System, 4th edition (Biaggioni, I., Browning, K., Fink, G., Jordan, J., Low, P.A., Paton, J.F.R., eds.), Academic Press, in press (2022).
Perry-Hauser, N.A., Hopkins, J.B., Zhuo, Y., Zheng, C., Perez, I., Schulz, K.M., Vishnivetskiy, S.A., Kaya, A.I., Sharma, P., Dalby, K.N., Chung, K.Y., Klug, C.S., Gurevich, V.V., Iverson, T.M. The two non-visual arrestins engage ERK2 differently. J Mol Biol 434, (7), 167465; doi: 10.1016/j.jmb.2022.167465 (2022).
Perez, I., Berndt, S., Agarwal, R., Castro, M.A., Vishnivetskiy, S.A., Smith, J.C., Sanders, C.R., Gurevich, V.V., Iverson, T.M. A model of the signal initiation complex between arrestin-3 and the Src family kinase Fgr. J Mol Biol 434, 167400; doi: 10.1016/j.jmb.2021.167400 (2022)
2021
Karnam, P., Vishnivetskiy, S.A., Gurevich, V.V. Structural basis of arrestin selectivity for active phosphorylated G protein-coupled receptors. Int J Mol Sci 22 (22), 12481; DOI: doi.org/10.3390/ijms222212481 (2021).
Klaus, C., Caruso, G., Gurevich, V.V., Hamm, H.E., Makino, C.L., DiBenedetto, E. Phototransduction in retinal cones: analysis of parameter importance. PLoS One 16 (10), e0258721; doi 1371/journal.pone.0258721 (2021).
Gurevich, V. V., Benovic, J. L., Gurevich, V.V. Chapter 00109. G Protein-Coupled Receptor Kinases and Arrestins. In: Jez Joseph (eds.) Encyclopedia of Biological Chemistry, 3rd Edition. vol. 6, pp. 423– Oxford: Elsevier. DOI: 10.1016/B978-0-12-819460-7.00109-2 (2021).
Gurevich V.V. Biology and structure of arrestin proteins [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. https://hstalks.com/bs/4663/ (2021).
Qu, C., Park, J.Y., Yun, M.W., He, Q.-T., Yang, F., Kim, K., Ham, D., Li, R.-R., Iverson, T.M., Gurevich, V.V., Sun, J.-P., Chung, K.Y. Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade. Proc Natl Acad Sci USA 118 (37), e2026491118; DOI 1073/pnas.2026491118 (2021).
Gurevich V.V., Gurevich E.V. Receptor-enzyme complex structures show how receptors start to switch off. Nature 595 (7868), 499-500; doi: 10.1038/d41586-021-01873-4 (2021).
Vishnivetskiy, S.A., Huh, E.K., Gurevich, E.V., Gurevich, V.V. The finger loop as an activation sensor in arrestin, 157 (4), 1138-1152; doi: 10.1111/jnc.15232 (2021).
Vishnivetskiy, S.A., Zheng, C., May, M.B., Karnam, P.C., Gurevich, E.V., Gurevich, V.V. Lysine in the lariat loop of arrestin does not serve as phosphate sensor. J Neurochem 156, 435-444; doi: 10.1111/jnc.15110 (2021).
Chen, Q., Zhuo, Y., Sharma, P., Perez, I., Francis, D.J., Chakravarthy, S., Vishnivetskiy, S.A., Berndt, S., Hanson, S.M., Zhan, X., Brooks, E.K., Altenbach, C., Hubbell, W.L., Klug, C.S., Iverson, T.M., Gurevich, V.V. An eight amino acid segment controls oligomerization and preferred conformation of the two non-visual arrestins. J Mol Biol 433 (4), 166790; doi: 10.1016/j.jmb.2020.166790 (2021).
Gurevich VV. Scholarly Community Encyclopedia, https://encyclopedia.pub/7370 (2021).
Seyedabadi, M., Gharghabi, M., Gurevich EV, Gurevich VV. Receptor-arrestin interactions: the GPCR perspective. Biomolecules 11 (2), 218; doi: 10.3390/biom11020218 (2021).
2020
Vogel, A., Bosse, M., Gauglitz, M., Wistuba, S., Schmidt, P., Kaiser, A., Gurevich, V.V.,
Beck-Sickinger, A.G., Hildebrand, P.W., Huster, D. The Dynamics of the Neuropeptide Y Receptor Type 1 Investigated by Solid-State NMR and Molecular Dynamics Simulation. Molecules, in press (2020).
Caruso, G., Klaus, C.J., Hamm, H.E., Gurevich, V.V., Makino, C.L., DiBenedetto, E. Position of rhodopsin photoisomerization on the disk surface confers variability to the rising phase of the single photon response in vertebrate rod photoreceptors. PLoS One 15 (10), e0240527; doi: 10.1371/journal.pone.0240527 (2020).
Gurevich V.V., Gurevich E.V. Designer adhesion GPCR tells it’s signaling story. Nat Chem Bio, in press; doi: 10.1038/s41589-020-00673-7 (2020).
Zhuo, Y., Gurevich, V.V., Vishnivetskiy, S.A., Klug, C. Marchese, A. A non-GPCR binding partner interacts with a novel surface on β-arrestin1 to mediate GPCR signaling. J Biol Chem 295 (41): 14111-14124; doi: 10.1074/jbc.RA120.015074 (2020).
Krug, U., Gloge, A., Schmidt, P., Baldus, J., Bernhard, F., Kaiser, A., Montag, C., Gauglitz, M., Vishnivetskiy, S.A., Gurevich, V.V., Beck-Sickinger, A.G., Glaubitz, C., Huster, D. The Conformational Equilibrium of the Neuropeptide Y2 Receptor. Angew Chem Int Ed Engl, in press; doi: 10.1002/anie.202006075 (2020).
Böttke, T., Ernicke, S., Serfling, R., Ihling, C., Burda, E., Gurevich, V.V., Sinz, A., Coin, I. Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers. EMBO Rep 21 (11): e50437; doi: 10.15252/embr.202050437 (2020).
Samaranayake, S., Vishnivetskiy, S.A., Shores, C.R., Thibeault, K.C., Kook, S.,Chen, J., Burns, M.E., Gurevich, E.V., Gurevich, V.V. Biological role of arrestin-1 oligomerization. J Neurosci 40 (42): 8055-8069; doi: 10.1523/JNEUROSCI.0749-20.2020 (2020).
Kook, S., Zhan, X., Thibeault, K., Ahmed, M.R., Gurevich, V.V., Gurevich, E.V. Mdm2 enhances ligase activity of parkin and facilitates mitophagy. Sci Rep 10 (1) 5028; doi: 10.1038/s41598-020-61796-4 (2020).
Kaya, A.I., Perry, N.A., Gurevich, V.V., Iverson, T.M. Phosphorylation barcode-dependent signal bias of the dopamine D1 receptor. Proc Natl Acad Sci USA 117 (25): 14139-14149; doi: 10.1073/pnas.1918736117 (2020).
Shieh, B.-H., Gurevich, E. V., and Gurevich, V. V. Receptor Adaptation Mechanisms. In: eLS. John Wiley & Sons, Ltd: Chichester; DOI: 10.1002/9780470015902.a0000052.pub3 (1920).
Gurevich, V. V., Benovic, J. L., Gurevich, V.V. Chapter 5046. G-Protein-Coupled Receptor Kinases and Arrestins. Encyclopedia of Biological Chemistry, 3rd Elsevier, in press (2020).
Gurevich, V.V., Gurevich, E.V. Biased GPCR signaling: possible mechanisms and inherent limitations. Pharm Ther 211, 107540; doi: 10.1016/j.pharmthera.2020.107540 (2020).
Gurevich, V.V., Gurevich, E.V. Targeting arrestin interactions with its partners for therapeutic purposes. Chapter 7 in: Adv Protein Chem Struct Biol. Protein interactions as targets in drug discovery. Ed: Rossen Donev. Elsevier, ISBN: 978-0-12-816846-2, Vol 121, 169-197 (2020).
2019
Caruso, G., Gurevich, V.V., Klaus, C., Hamm, H., Makino, C.L., DiBenedetto, E. Local, non-linear effects of cGMP and Ca2+ reduce single photon response variability in retinal rods. PLoS One 14 (12): e0225948. doi: 10.1371/journal.pone.0225948 (2019).
Meister, J., Bone, D.B.J., Godlewski, G., Liu, Z., Lee, R.J., Vishnivetskiy, S.A., Gurevich, V.V., Springe,r D., Kunos, G., Wess, J. Metabolic effects of skeletal muscle-specific deletion of beta-arrestin-1 and -2 in mice. PLoS Genet. 2019 Oct 17;15(10) e1008424, doi: 10.1371/journal.pgen.1008424 (2019).
Gurevich, V.V. Protein multi-functionality: introduction. Cell Mol Life Sci 76, 4405-4406; doi: 10.1007/s00018-019-03271-6 (2019).
Gurevich, V.V., Gurevich, E.V. Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies. Cell Mol Life Sci 76, 4413-4421; doi: 10.1007/s00018-019-03272-5 (2019).
Gurevich, V.V., Gurevich, E.V. Receptors talking: solo vs chorus. Atlas of science https://atlasofscience.org/receptors-talking-solo-vs-chorus/ (2019).
Perry, N.A., Fialkowski, K.P., Kaoud, T.S., Kaya, A.I., Chen, A.L., Taliaferro, J.M., Gurevich, V.V., Dalby, K.N., Iverson, T.M. Arrestin-3 interaction with maternal embryonic leucine-zipper kinase. Cell Signal, 63, 109366; doi: 10.1016/j.cellsig.2019.109366 (2019).
Barella, L.F., Rossi, M., Zhu, L., Cui, Y., Cheng, X., Chen, W., Gurevich, V.V., Wess, J. Beta- cell-intrinsic β-arrestin-1 signaling enhances sulfonylurea-induced insulin secretion. J Clin Invest 130, 3732-3737; doi: 10.1172/JCI126309 (2019).
Klaus, C., Caruso, G., Gurevich, V.V., DiBenedetto, E. Multi-scale numerical modeling of spatio-temporal signaling in cone phototransduction. PLoS One 14 (7), e0219848; doi: 10.1371/journal.pone.0219848 (2019).
Sammons, R.M., Perry, N.A., Li, Y., Cho, E.J., Piserchio, A., Zamora-Olivares, D.P., Ghose, R., Kaoud, T.S., Debevec, G., Bartholomeusz, C., Gurevich, V.V., Iverson, T.M., Giulianotti, M., Houghten, R.A., Dalby, K.N. A Novel Class of Common Docking Domain Inhibitors That Prevent ERK2 Activation and Substrate Phosphorylation. ACS Chem Biol 14 (6), 1183-1194; doi: 10.1021/acschembio.9b00093 (2019)
Berndt, S., Gurevich, V.V., Iverson, T.M. Crystal structure of the SH3 domain of human Lyn non-receptor tyrosine kinase. PLoS One 14 (4), e0215140; doi: 10.1371/journal.pone.0215140 (2019).
Zheng, C., Tholen, J. Gurevich, V.V. Critical role of the finger loop in arrestin binding to the receptors. PLoS One 14 (3), e0213792; doi: 10.1371/journal.pone.0213792 (2019).
Gurevich, V.V., Gurevich, E.V. GPCR signaling regulation: the role of GRKs and arrestins. Front Pharmacol 10, 125; org/10.3389/fphar.2019.00125 (2019).
Gurevich V.V., Gurevich E.V. The structural basis of the arrestin binding to GPCRs. Mol Cell Endocrinol 484, 34-41; doi: 10.1016/j.mce.2019.01.019 (2019).
Perry, N.A., Zhan, X., Gurevich, E.V., Iverson, T.M., Gurevich, V.V. Using in vitro pull-down and in cell overexpression assays to study protein interactions with arrestins, pp. 107-120. In: Beta-arrestins: Methods and protocols, M. G. Scott, S. A. Laporte, Eds. Springer-Verlag, Berlin-Heidelberg DOI: 10.1007/978-1-4939-9158-7_7 (2019).
Perry, N.A., Kaoud, T.S., Ortega, O.O., Kaya, A.I., Marcus, D.J., Pleinis, J.M., Berndt, S., Chen, Q., Zhan, X., Dalby, K.N., Lopez, C.F., Iverson, T.M., Gurevich, V.V. Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification. Proc Natl Acad Sci USA 116 (3), 810-815; https://doi.org/10.1073/pnas.1819230116 (2019).
Kook, S., Vishnivetskiy, S.A., Gurevich, V.V., Gurevich, E.V. Cleavage of arrestin-3 by caspases attenuates cell death by precluding arrestin-dependent JNK activation. Cell Signal 54, 161-169; doi: 10.1016/j.cellsig.2018.11.023 (2019).
Gurevich, V.V., Gurevich, E.V. Arrestin mutations: some cause diseases, others promise cure. Prog Mol Biol Transl Sci 161, 29-45; https://doi.org/10.1016/bs.pmbts.2018.09.004 (2019).
2018
Gurevich, V.V., Gurevich, E.V. Arrestin-mediated signaling: is there a controversy? World J Biol Chem 9 (3) 25-35 (2018). DOI: https://dx.doi.org/10.4331/wjbc.v9.i3.25
Gurevich, V.V., Gurevich, E.V. Arrestins and G proteins in cellular signaling: the coin has two sides. Sci Signal 11 (549), eaav1646; doi: 10.1126/scisignal.aav1646 (2018).
Samaranayake, S., Song, X., Vishnivetskiy. S.A., Chen, J., Gurevich, E.V., Gurevich, V.V. Enhanced mutant compensates for defects in rhodopsin phosphorylation in the presence of endogenous arrestin-1. Front Mol Neurosci 11, 203; doi: 10.3389/fnmol.2018.00203 (2018).
Gurevich, V.V. Protein Flexibility and Cellular Signaling. EC Pharmacology and Toxicology6, 384-389 (2018).
Gurevich, V.V., Chen, Q., Gurevich, E.V. Arrestins: introducing signaling bias into multi-functional proteins. Prog Mol Biol Transl Sci 160, 47-61; doi: 10.1016/bs.pmbts.2018.07.007 (2018)
Gurevich, V.V., Gurevich, E.V. GPCRs and signal transducers: interaction stoichiometry. Trands Pharm Sci 39 (7), 672-684; doi: 10.1016/j.tips.2018.04.002 (2018).
Gurevich, V.V. Protein Flexibility and Cellular Signaling. EC Pharmacology and Toxicology 6.6, 384-389 (2018).
Chen, Q., Iverson, T.M., Gurevich, V.V. Structural basis of arrestin-dependent signal transduction. Trends Biochem Sci 43 (6), 412-423; doi: 10.1016/j.tibs.2018.03.005 (2018).
Gurevich, V.V., Gurevich, E.V., and Uversky, V.N. Arrestins: structural disorder creates rich functionality. Protein Cell 9 (12), 986-1003; doi: 10.1007/s13238-017-0501-8 (2018).
Vishnivetskiy, S.A., Sullivan, L.S., Bowne, S.J., Daiger, S.P., Gurevich, E.V., Gurevich, V.V. Molecular defects of the disease-causing human arrestin-1 C147F mutants. Invest Ophthalmol Vis Sci 59 (1), 13-20; doi: 10.1167/iovs.17-22180 (2018).
Toth, A.D., Prokop, S., Gyombolai, P., Varnai, P., Balla, A., Gurevich, V.V., Hunaydi, L., Turu, G. Heterologous phosphorylation-induced formation of a stability lock permits regulation of inactive receptors by b-arrestins. J Biol Chem 293 (3), 876-892; doi: 10.1074/jbc.M117.813139 (2018).
Tso, S.-C., Chen, Q., Vishnivetskiy, S.A., Gurevich, V.V., Iverson T.M., Brautigam, C.A. Using two-site binding models to analyze microscale thermophoresis data. Anal Biochem 540-541, 64-75; doi: 10.1016/j.ab.2017.10.013 (2018).
Cleghorn, W.M., Bulus, N., Kook, S., Gurevich, V.V., Zent, R., Gurevich, E. V. Non-visual arrestins regulate the focal adhesion formation via small GTPases RhoA and Rac1 independently of GPCRs. Cell Signal 42, 259-269; doi: 10.1016/j.cellsig.2017.11.003 (2018).
2017
Gurevich, V.V. and Gurevich, E.V. Molecular mechanisms of GPCR signaling Int J Mol Sci 18, 2519; doi:10.3390/ijms18122519 (2017).
Cleghorn, W.M., Bulus, N., Kook, S., Gurevich, V.V., Zent, R., Gurevich, E. V. Non-visual arrestins regulate the focal adhesion formation via small GTPases RhoA and Rac1 independently of GPCRs. Cell Signal 42, 259-269; doi: 10.1016/j.cellsig.2017.11.003 (2017).
Chen, Q., Perry, N.A., Vishnivetskiy, S.A., Berndt, S., Gilbert, N.C., Zhuo, Y., Singh, P.K., Tholen, J., Ohi, M.D., Gurevich, E.V., Brautigam, C.A., Klug, C.S., Gurevich, V.V., Iverson, T.M. Structural basis of arrestin-3 activation and signaling. Nat Commun 8, 1427; doi: 10.1038/s41467-01701218-8 (2017).
Indrischek, H., Prohaska, S.J., Gurevich, V.V., Gurevich, E.V., Stadler, P.F. Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes. BMC Evol. Biol. 17(1): 163; doi: 10.1186/s12862-017-1001-4 (2017).
Vishnivetskiy SA, Lee RJ, Zhou XE, Franz A, Xu Q, Xu HE, Gurevich VV. Functional role of the three conserved cysteines in the N-domain of visual arrestin-1. J Biol Chem, 292 (30), 12496-12502; doi: 10.1074/jbc.M117.790386 (2017).
Zhou, X.E., He, Y., de Waal, P.W., Gao, X., Kang, Y., Van Eps, N., Yin, Y., Pal, K., Goswami, D., White, T.A., Barty, A., Latorraca, N.R., Chapman, H.N., Hubbell, W.L., Dror, R.O., Stevens, R.C., Cherezov, V., Gurevich, V.V., Griffin, P.R., Ernst, O.P., Melcher, K., Xu, H.E. Structural Identification of Phosphorylation Codes for Arrestin Recruitment by G protein-Coupled Receptors. Cell 170 (3), 457-469.e13; doi: 10.1016/j.cell.2017.07.002 (2017).
Zhu, L., Rossi, M., Cui, Y., Lee, R.J., Sakamoto, W., Perry, N.A., Urs, N.M., Caron, M.G., Gurevich, V.V., Godlewski, G., Kunos, G., Chen, M., Chen, W., Wess, J. Hepatic b-arrestin-2 is essential for maintaining euglycemia. J Clin Invest 127 (8), 2941-2945; doi: 10.1172/JCI92913 (2017).
Prokop, S., Perry, N.A., Vishnivetskiy, S.A., Toth, A.D., Inoue, A., Milligan, G., Iverson, T.M., Hunyady, L., Gurevich, V.V. Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors. Cell Signal 36, 98-107; doi: 10.1016/j.cellsig.2017.04.021 (2017).
Sullivan, L.S., Bowne, S.J., Koboldt, D.C., Cadena, E.L., Heckenlively, J.R., Branham, K.E., Birch, D.G., Wheaton, D.H., Jones, K.D., Ruiz, R.S., Pennesi, M., Northrup, H., Gurevich, V.V., Xu, M., Li, Y., Chen, R., Daiger, S.P. A novel dominant mutation in SAG, the arrestin-1 gene, is a common cause of retinitis pigmentosa in Hispanic families in the Southwestern United States. Invest Ophthalmol Vis Sci 58 (5), 2774-2784; doi: 10.1167/iovs.16-21341 (2017).
Zurkovsky, L., Sedaghat, K., Ahmed, M.R., Gurevich, V.V., Gurevich, E.V. Arrestin-2 and arrestin-3 differentially modultae locomotor responses and sensitization to amphetamine. Neuropharmacology 121, 20-29; doi: 10.1016/j.neuropharm.2017.04.021 (2017).
Gurevich, V.V. and Gurevich, E.V. Arrestins: discovery of the family and functional role of conformational flexibility. Ch 1 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Spiller, B.W., Zhan, X., Gurevich, V.V. Arrestin-3: the structural basis of lower receptor selectivity. Ch 5 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Wiener, R, Vishnivetskiy, S.A., Gurevich, V.V., Hirsch, J.A. Phosphate sensor and construction of phosphorylation-independent arrestins. Ch 6 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Vishnivetskiy, S.A., Hubbell, W.L., Klug, C.S., Gurevich, V.V. GPCR footprint on arrestins and manipulation of receptor specificity. Ch 10 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Bandyopadhyay, A., Zhuo, Y., Hubbell, W.L., Klug, C.S., Gurevich, V.V., Ernst, O.P. Active conformations of arrestins: expected and unexpected changes. Ch 12 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Kang, Y, Melcher, K., Gurevich, V.V., Xu, H.E. The arrestin-receptor complex: exciting answers and new questions. Ch 13 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Zhan, X., Gurevich, V.V., Gurevich, E.V. Scaffolding c-Jun N-terminal kinase cascades: mechanistic insights from the reconstituted arrestin-JNK cascades. Ch 14 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Perry, N.A., Zhan, X., Iverson, T.M., Gurevich, E.V., Gurevich, V.V. Monofunctional elements of multi-functional arrestin proteins. Ch 18 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Berndt, S., Gurevich, V.V., Gurevich, E.V. Arrestins in cell death. Ch 19 in The structural basis of arrestin functions. Springer-Verlag, Berlin-Heidelberg, ISBN 978-3-319-57552-0 (2017).
Zhu, L., Almaça, J., Dadi, P.K., Hong, H., Sakamoto, W., Rossi, M., Lee, R.J., Vierra, N.C. Lu, H., Cui, Y., McMillin, S.M., Perry, N.A., Gurevich, V.V., Lee, A., Kuo, B., Leapman, R.D., Matschinsky, F.M., Doliba, N.M., Urs, N.M., Caron, M.G., Jacobson, D.A., Caicedo, A., Wess, J. b-Arrestin-2 is an essential regulator of pancreatic b-cell function under physiological and pathophysiological conditions. Nat Commun 8, 14295; DOI 10.1038/NCOMMS14295 (2017).
Gurevich, V.V. and Gurevich, E.V. Phototransduction: inactivation in rods. Chapter 01477 in Reference Module in Neuroscience and Biobehavioral Psychology, Elsevier, 2017. ISBN 9780128093245 (2017).
Gurevich, V.V. and Gurevich, E.V. Phototransduction: inactivation in cones. Chapter 01476 in Reference Module in Neuroscience and Biobehavioral Psychology, Elsevier, 2017. ISBN 9780128093245 (2017).
Wanka, L., Babilon, S., Burket, K., Morl, K., Gurevich, V.V., Beck-Sickinger, A.G. C-terminal motif of human neuropeptide Y4 receptor determines internalization and arrestin recruitment. Cell Signal 29, 233-239 (2017).
2016
Gurevich, V.V. and Gurevich, E.V. G protein-coupled receptor kinases (GRKs) history: evolution and discovery. In: G protein-coupled receptor kinases. Eds: V.V. Gurevich, E. V. Gurevich and J. G. Tesmer. Springer-Verlag, Berlin-Heidelberg, pp. 3-22 (2016).
Gurevich, E.V., Gainetdinov, R.R. and Gurevich, V.V. Regulation of dopamine-dependent behaviors by G protein-coupled receptor kinases. In: G protein-coupled receptor kinases. Eds: V.V. Gurevich, E. V. Gurevich and J. G. Tesmer. Springer-Verlag, Berlin-Heidelberg, pp. 237-269 (2016).
Gurevich, E.V., Gainetdinov, R.R., Gurevich, V.V. G protein-coupled receptor kinases as regulators of dopamine receptor functions. Pharmacol Res. 111, 1-16; doi: 10.1016/j.phrs.2016.05.010 (2016).
Zhan, X., Stoy, H., Kaoud, T.S., Perry, N.A., Chen, Q., Perez, A., Els-Heindl, S., Slagis, J.V., Iverson, T.M., Beck-Sickinger, A.G., Gurevich, E.V., Dalby, K.N., Gurevich, V.V. Peptide mini-scaffold facilitates JNK3 activation in cells. Sci Rep 6, 21025; doi: 10.1038/srep21025 (2016).
Hu, J., Stern, M., Gimenez, L.E., Wanka, L., Zhu, L., Rossi, M., Meister, J., Inoue, A., Beck-Sickinger, A.G., Gurevich, V.V., Wess, J. A G protein-biased designer G protein-coupled receptor useful for studying the physiological relevance of Gq/11-dependent signaling pathways. J Biol Chem 291 (15), 7809-20 (2016). JBC paper of the week.
Gurevich V.V. Paradigm shift is the normal state of pharmacology. EC Pharmacol Toxicol 2 (2), 80-85 (2016).
2015
Chatterjee D, Eckert CE, Slavov C, Saxena K, Fürtig B, Sanders CR, Gurevich VV, Wachtveitl J, Schwalbe H. Influence of arrestin on the photodecay of bovine rhodopsin. Angew Chem Int Ed Engl 54 (46), 13555-60; doi: 10.1002/anie.201505798 (2015).
Nakajima, K.-I, Gimenez, L.E.D., Gurevich, V.V., Wess, J. Design and analysis of arrestin-biased DREADD. Chapter 2 in Designer receptors exclusively activated by designer drugs. Thiel, G. (ed). Neoromethods, v 108, pp. 29-48.
Chang, S.D., Mascarella, S. W., Spangler, S.M., Gurevich, V.V., Navarro, H.A., Carroll, F.I., Bruchas, M.R. Quantitative Signaling and Structure-Activity Analyses Demonstrate Functional Selectivity at the Nociceptin/Orphanin FQ Opioid Receptor. Mol Pharmacol 88 (3), 502-11 (2015).
Inagaki, S., Ghirlando, R., Vishnivetskiy, S.A., Homan, K.T., White, J.F., Tesmer, J.J., Gurevich, V.V., Grisshammer, R. G protein-coupled receptor kinase 2 (GRK2) and 5 (GRK5) exhibit selective phosphorylation of the neurotensin receptor in vitro. Biochemistry 54 (28), 4320-9 (2015).
Kang, Y., Zhou, X.E., Gao, X., He, Y., Liu, W., Ishchenko, A., Barty, A., White, T.A., Yefanov, O., Han, G.W., Xu, Q., de Waal, P.W., Ke, J., Tan, M.H.E., Zhang, C., Moeller, A., West, G.M., Van Eps, N., Caro, L.N., Vishnivetskiy, S.A., Lee, R.J., Suino-Powell, K.M., Gu, X., Pal, K., Ma, J., Zhi, X., Boutet, S., Williams, G.J., Messerschmidt, M., Gati, C., Zatsepin, N.A., Wang, D., James, D., Basu, S., Roy-Chowdhury, S., Conrad, C., Coe, J., Liu, H., Lisova, S., Kupitz, C., Grotjohnn, I., Fromme, R., Jiang, Y., Tasn, M., Yang, H., Li, J., Wang, M., Li, D., Zhao, Y., Standfuss, J., Diederichs, K., Potter, C.S., Carragher, B., Caffrey, M., Jiang, H., Chapman, H.N., Spence, J.C.H., Fromme, P., Weierstall, U., Ernst, O.P., Gurevich, V.V., Griffin, P.R., Hubbell, W.L., Stevens, R.C., Cherezov, V., Melcher, K., Xu, H.E. Crystal structure of rhodopsin bound to arrestin determined by femtosecond X-ray laser. Nature, 523 (7562), 561-7. doi: 10.1038/nature14656 (2015).
Donthamsetti, P., Quejada, J.R., Javitch, J.A., Gurevich V.V., Lambert, N.A. Using bioluminescent resonance energy transfer (BRET) to characterize agonist-induced arrestin recruitment to modified and unmodified G protein-coupled receptors (GPCRs). Curr Protoc Pharmacol 70, 2.14.1-2.14.14; doi: 10.1002/0471141755.ph0214s70 (2015).
Gurevich, V.V. and Gurevich, E.V. Analyzing the roles of multi-functional proteins in cells: the case of arrestins and GRKs. Crit Rev Biochem Mol Biol 50 (5), 440-52 (2015).
Gurevich, V.V. and Gurevich, E.V. Arrestins: critical players in trafficking of many GPCRs. Prog Mol Biol Transl Sci 132, 1-14 (2015).
Ahmed, M.R., Bychkov, E., Li, L., Gurevich, V.V., Gurevich, E.V. GRK3 suppresses L-DOPA-induced dyskinesia in the rat model of Parkinson’s disease via its RGS homology domain. Sci Rep 5, 10920; doi: 10.1038/srep10920 (2015).
Azevedo, A.W., Doan, T., Moaven, H., Sokal, I., Baameur, F., Vishnivetskiy, S.A., Homan, K.T., Tesmer, J.J.G., Gurevich, V.V., Chen, J., Rieke, F. C-terminal Threonines and Serines Play Distinct Roles in the Desensitization of Rhodopsin, a G protein-Coupled Receptor. eLife 4: e05981 (2015). doi: 10.7554/eLife.05981.
Heifetz A, Schertler GF, Seifert R, Tate CG, Sexton PM, Gurevich VV, Fourmy D, Cherezov V, Marshall FH, Storer RI, Moraes I, Tikhonova IG, Tautermann CS, Hunt P, Ceska T, Hodgson S, Bodkin MJ, Singh S, Law RJ, Biggin PC. GPCR structure, function, drug discovery and crystallography: report from academia-industry international conference (UK Royal Society) Chicheley Hall, 1-2 September 2014. Naunyn Schmiedebergs Arch Pharmacol 388(8):883-903; doi: 10.1007/s00210-015-1111-8 (2015).
Stoy, H. and Gurevich, V.V. How genetic errors in GPCRs affect their function: possible therapeutic strategies. Genes Dis 2, 108-132 (2015).
Gurevich, V.V. and Gurevich, E.V. Beyond traditional pharmacology: new tools and approaches. Br J Pharmacol 172, 3229–324; doi: 10.1111/bph.13066 (2015).
Li L, Homan KT, Vishnivetskiy SA, Manglik A, Tesmer JJ, Gurevich VV, Gurevich EV. G ptotein-coupled receptor kinases of the GRK4 protein subfamily phosphorylate inactive G protein-coupled receptors (GPCRs). J Biol Chem 290 (17), 10775-10790 (2015).
Berkowitz, B.A., Gorgis, J., Patel, A., Baameur, F., Gurevich, V.V., Craft, C.M., Kefalov, V.J., Roberts, R. Development of an MRI biomarker sensitive to tetrameric visual arrestin 1 and its reduction via light-evoked translocation in vivo. FASEB J. 29 (2), 554-564 (2015).
Cleghorn, W.M., Branch, K.M., Kook, S., Arnette, C., Bulus, N., Zent, R., Kaverina, I., Gurevich, E.V., Weaver, A.M. Gurevich, V.V. Arrestins regulate cell spreading and motility via focal adhesion dynamics. Mol Biol Cell, 26 (4), 622-635 (2015).
Chen, Q., Vishnivetskiy, S.A., Zhuang, T., Cho, M.-K., Thaker, T.M., Sanders, C.R., Gurevich, V.V., Iverson, T.M. The rhodopsin-arrestin-1 interaction in bicelles. Chapter 6 in Rhodopsin: Methods and Protocols (Beata Jastrzebska, ed.), Methods in Molecular Biology, vol. 1271, pp. 77-95; Springer, New York (2015).
Zhan, X., Kook, S., Kaoud, T.S., Dalby, K.N., Gurevich, E.V., and Gurevich, V.V. 2015. Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs). Curr Protoc Pharmacol 68:2.12.1-2.12.26. doi: 10.1002/0471141755.ph0212s68 (2015).
2014
Gurevich, V.V. and Gurevich, E.V. Overview of Different Mechanisms of Arrestin-Mediated Signaling. Curr Protoc Pharmacol 67, 2.10.1-9 (2014).
Vishnivetskiy S.A., Zhan, X., Chen, Q., Iverson, T.M., Gurevich VV. Arrestin expression in E. coli and purification. Curr Protoc Pharmacol 67, 2.11.1-2.11.19 (2014).
Mäde, V., Babilon, S., Jolly, N., Wanka, L., Bellmann-Sickert, K., Giminez, L.E., Mörl, K., Cox, H.M., Gurevich, V.V., Beck-Sickinger, A.G. Peptide Modifications Differentially Alter G Protein-Coupled Receptor Internalization and Signaling Bias, Angew Chem Int Ed Engl, 53 (38), 10067-10071 (2014).
Zhuo, Y., Vishnivetskiy, S.A., Zhan, X., Gurevich, V.V., Klug, C.S. Identification of receptor binding-induced conformational changes in non-visual arrestins. J Biol Chem 289 (30), 20991-21002 (2014).
Gurevich, V.V. and Gurevich, E.V. Design of super-arrestins for gene therapy of diseases associated with excessive signaling of G protein-coupled receptors. Ch 14 in: G protein-coupled receptor genetics: research and methods in post-genomic era. Craig W. Stevens, Ed. Springer Protocols, Methods in Pharmacology and Toxicology. Humana Press, Springer Science+Business Media, NY (2014).
Gurevich, V.V. and Gurevich, E.V. Arrestin makes T cell stop and become active. EMBO J 33 (6) 531-533 (2014).
Gimenez, L.E., Babilon, S., Wanka, L., Beck-Sickinger, A.G., Gurevich, V.V. Mutations in arrestin-3 differentially affect binding to neuropeptide Y receptor subtypes. Cell Signal 26 (7), 1523-1531 (2014).
Zhan, X., Perez, A., Gimenez, L.E., Vishnivetskiy, S.A., Gurevich, V.V. Arrestin-3 binds the MAP kinase JNK3a2 via multiple sites on both domains. Cell Signal 26 (4), 766-776 (2014).
Kook, S., Zhan X., Cleghorn, W.M., Benovic, J.L., Gurevich, V.V., Gurevich, E.V. Caspase-cleaved arrestin-2 and BID cooperatively facilitate cytochrome C release and cell death. Cell Death Differ 21 (1), 172-84 (2014). doi: 10.1038/cdd.2013.143
Gurevich, V.V. and Gurevich, E.V. Extensive shape shifting underlies functional versatility of arrestins. Curr Opin Cell Biol 27, 1-9 (2014).
Gurevich, E.V. and Gurevich, V.V. Therapeutic potential of small molecules and engineered proteins. In: Arrestins – Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology 219, p. 1-12, Springer-Verlag, Berlin-Heidelberg (2014).
Gurevich, V.V., Song, X., Visnivetskiy, S.A., Gurevich, E.V. Enhanced phosphorylation-independent arrestins and gene therapy. In: Arrestins – Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology 219, p. 133-152, Springer-Verlag, Berlin-Heidelberg (2014).
Gimenez, L.E., Vishnivetskiy, S.A., and Gurevich, V.V. Targeting individual GPCRs with redesigned non-visual arrestins. In: Arrestins – Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology 219, p. 153-170, Springer-Verlag, Berlin-Heidelberg (2014).
Chen, Q., Zhuo, Y., Kim, M., Hanson, S.M., Vishnivetskiy, S.A., Altenbach, C., Klug, C.S., Hubbell, W.L., and Gurevich, V.V. Self-association of arrestin family members. In: Arrestins – Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology 219, p. 205-223, Springer-Verlag, Berlin-Heidelberg (2014).
Zhan, X., Kook, S., Gurevich, E.V. and Gurevich, V.V. Arrestin-dependent activation of JNK family kinases. In: Arrestins – Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology 219, p. 259-280, Springer-Verlag, Berlin-Heidelberg (2014).
Kook, S., Gurevich, V.V. and Gurevich, E.V. Arrestins in apoptosis. In: Arrestins – Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology 219, p. 309-339, Springer-Verlag, Berlin-Heidelberg (2014).
2013
Kook, S., Zhan, X., Kaoud, T.S., Dalby, K.N., Gurevich, V.V., Gurevich, E.V. Arrestin-3 binds c-Jun N-terminal kinase 1 (JNK1) and JNK2 and facilitates the activation of these ubiquitous JNK isoforms in cells via scaffolding. J Biol Chem 288 (52), 37332-37342 (2013).
Zhan, X., Kaoud, T.S., Kook, S., Dalby, K.N., Gurevich, V.V. JNK3 enzyme binding to arrestin-3 differentially affects the recruitment of upstream mitogen-activated protein kinase kinases. J Biol Chem 288 (40), 28535-28547 (2013).
Song, X., Seo, J., Baameur, F., Vishnivetskiy, S.A., Chen, Q., Kook, S., Kim, M., Brooks, E.K., Altenbach, C., Hong, Y., Hanson, S.M., Palazzo, M.C., Chen, J., Hubbell, W.L., Gurevich, E.V., Gurevich, V.V. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant. Cell Signal 25, 2613-2624 (2013).
Vishnivetskiy, S.A., Ostermaier, M.K., Singhal, A., Panneels, V., Homan, K.T., Glukhova, A., Sligar, S.G., Tesmer, J.J.G., Schertler, G.F.X., Standfuss, J., Gurevich, V.V. Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding. Cell Signal 25 (11), 2155-2162 (2013).
Moaven, H., Koike, Y., Jao, C., Gurevich, V.V., Langen, R., Chen, J. Visual arrestin interaction with clathrin adaptor AP2 regulates photoreceptor survival in the vertebrate retina. Proc. Natl. Acad. Sci. USA 110 (23), 9463-9468 (2013).
Vishnivetskiy, S.A., Baameur, F., Findley, K.R., Gurevich, V.V. Critical role of central 139-loop in stability and binding selectivity of arrestin-1. J Biol Chem 288 (17), 11741-50 (2013).
Singhal, A., Ostermaier, M.K., Vishnivetskiy, S.A., Panneels, V., Homan, K.T., Tesmer, J.J.G., Veprintsev, D., Deupi, X., Gurevich, V.V., Schertler, G.F.X., Standfuss, J. Insightes into congenital stationary night blindness based on the structure of G90D rhodopsin. EMBO Rep 14 (6), 520-526 (2013).
Gurevich, V.V. and Gurevich, E.V. Structural determinants of arrestin functions. Chapter 3 in The Molecular Biology of Arrestins, Luttrell, L.M., volume Editor. P. M. Conn, Series Editor. UK: Academic Press, Elsevier. Prog Mol Biol Transl Sci 118, 57-92 (2013).
Vishnivetskiy, S.A., Chen, Q., Palazzo, M.C., Brooks, E.K., Altenbach, C., Iverson, T.M., Hubbell, W.L., Gurevich, V.V. Engineering visual arrestin-1 with special functional characteristics. J Biol Chem 288 (5), 3394-3405 (2013).
Chen, Y.-J., Oldfield, S., Butcher, A.J., Tobin, A.B., Saxena, K., Gurevich, V.V., Benovic, J.L., Henderson, G., Kelly, E. Identification of phosphorylation sites in the COOH-terminal tail of the m-opioid receptor. J Neurochem 124 (2), 189-199 (2013).
Zhuang, T., Chen, Q., Cho, M.-K., Vishnivetskiy, S.A., Iverson, T.M., Gurevich*, V.V., Sanders*, C.R. (*corresponding authors). Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc. Natl. Acad. Sci. USA 110 (3), 942-947 (2013).
2012
Schattauer, S.S., Miyatake, M., Shankar, H., Zietz, C., Levin, J.R., Liu-Chen, L.Y., Gurevich, V.V., Rieder, M.J., Chavkin, C. Ligand directed signaling differences between rodent and human kappa opioid receptors. J Biol Chem 287, 41595-41607 (2012).
Kim, M., Vishnivetskiy, S.A., Van Eps, N., Alexander, N.S., Cleghorn, W.M., Zhan, X., Hanson, S.M., Morizumi, T., Ernst, O.P., Meiler*, J., Gurevich*, V.V., Hubbell*, W.L. (*corresponding authors) Conformation of receptor-bound visual arrestin. Proc. Natl. Acad. Sci. USA 109, 18407-18412 (2012).
Gimenez, L.E., Vishnivetskiy, S.A., Baameur, F., Gurevich, V.V. Manipulation of very few receptor-dicriminator residues greatly enhances receptor specificity of non-visual arrestins. J Biol Chem 287, 29495-29505 (2012).
Breitman, M., Kook, S., Gimenez, L.E., Lizama, B.N., Palazzo, M.C., Gurevich, E.V., Gurevich, V.V. Silent scaffolds: inhibition of c-Jun N-terminal kinase 3 activity in the cell by a dominant-negative arrestin-3 mutant. J Biol Chem 287, 19653-19664 (2012).
Aguila, B., Coulbault, L., Davis, A., Marie, N., Hasbi, A., Le Bras, F., Tóth, G., Borsodi, A., Gurevich, V.V., Jauzac, P., Allouche, S. bArrestin1-biased agonism at human d-opioid receptor by peptidic and alkaloid ligands. Cell Signal 24, 699-707 (2012).
Gimenez, L.E., Kook, S., Vishnivetskiy, S.A., Ahmed, M.R., Gurevich, E.V., Gurevich, V.V. The role of receptor-attached phosphates in the binding of visual and non-visual arrestins to G protein-coupled receptors. J Biol Chem 287, 9028-9040 (2012).
Mushegian, A., Gurevich V.V., Gurevich, E.V. The origin and evolution of G protein-coupled receptor kinases. PLoS One 7(3), e33806. doi:10.1371/journal.pone.0033806 (2012).
Gurevich, E.V., Tesmer, J.J.G., Mushegian, A., Gurevich, V.V. G protein-coupled receptor kinases: More than just kinases and not only for GPCRs. Pharmacol Ther 133, 40-69 (2012).
2011
Gurevich, V.V. and Gurevich, E.V. Chapter 17. The mechanics of arrestin-receptor interaction: how GPCRs and arrestins talk to each other. In “G protein-coupled receptors: From structure to function” (Eds. Jesús Giraldo and Jean-Philippe Pin), The Royal Society of Chemistry, pp. 335-358 (2011).
Gurevich, V.V., Hanson, S.M., Song, X., Vishnivetskiy, S.A., Gurevich, E.V. The functional cycle of visual arrestins in photoreceptor cells. Prog Retin Eye Res 30, 405-430 (2011). Doi: 10.1016/j.preteyeres.2011.07.002
Kim, M., Hanson, S.M., Vishnivetskiy, S.A., Song, X., Cleghorn, W.M., Hubbell, W.L., Gurevich, V.V. Robust self-association is a common feature of mammalian visual arrestin-1. Biochemistry 50, 2235-2242 (2011).
Ahmed, M.R., Zhan, X., Song, X., Kook, S., Gurevich, V.V., Gurevich, E.V. Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination. Biochemistry 50, 3749-3763 (2011).
Vishnivetskiy, S.A., Gimenez, L.E., Francis, D.J., Hanson, S.M., Hubbell, W.L., Klug, C.S., Gurevich, V.V. Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. J Biol Chem 286, 24288-24299 (2011).
Caruso, G., Bisegna, P., Andreucci, D., Lenoci, L., Gurevich, V.V., Hamm, H.E., DiBenedetto, E. Identification of key factors that reduce the variability of the single photon response. Proc. Natl. Acad. Sci. USA 108, 7804-7807 (2011).
Seo, J., Tsakem, E.L., Breitman, M., and Gurevich, V.V. Identification of arrestin-3-specific residues necessary for JNK3 activation. J Biol Chem 286, 27894-27901 (2011).
*Coffa, S., Bretman, M., Spiller, B.W., and Gurevich, V.V. A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding. Biochemistry 50, 6951-6958 (2011). *Highlighted on the Biochemistry home page.
Cleghorn, W.M., Tsakem, E.L., Song, X., Vishnivetskiy, S.A., Seo, J., Chen, J., Gurevich, E.V., and Gurevich, V.V. Progressive reduction of its expression in rods reveales two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery. PLoS One 6 (7), e22797 (2011).
Bychkov, E.R., Ahmed, M.R., Gurevich, V.V., Benovic, J.L., Gurevich, E.V. Reduced expression of G protein-coupled receptor kinases in schizophrenia but not in schizoaffective disorder. Neurobiol Dis 44, 248-258 (2011).
*Zhan, X., Kaoud, T.S., Dalby, K.N., Gurevich, V.V. Non-visual arrestins function as simple scaffolds assembling MKK4-JNK3a2 signaling complex. Biochemistry 50, 10520-10529 (2011). *Highlighted on the Biochemistry home page.
Coffa, S., Breitman, M., Hanson, S.M., Callaway, K., Kook, S., Dalby, K.N., Gurevich, V.V. The effect of arrestin conformation on the recruitment of C-Raf1, MEK1, and ERK1/2 activation. PLoS One 6(12), e28723 (2011).
Zhan, X., Gimenez, L.E., Gurevich, V.V., Spiller B.W. Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol 406, 467-478 (2011).
Song, X., Vishnivetskiy, S.A., Seo, J., Chen, J., Gurevich, E.V., Gurevich, V.V. Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health. Neuroscience 174, 37-49 (2011).
Bayburt, T.H., Vishnivetskiy, S.A., McLean, M.A., Morizumi, T., Huang, C.-c., Tesmer, J.J.G., Ernst, O.P., Sligar, S.G., Gurevich, V.V. Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J Biol Chem 286, 1420-8 (2011).
2010
Walther, C., Nagel, S., Gimenez, L.E., Morl, K., Gurevich, V.V., Beck-Sickinger, A.G. Ligand induced internalization and recycling of the human neuropeptide Y2 receptor is regulated by its C-terminal tail. J Biol Chem 285, 41578-41590 (2010).
Caruso, G., Bisegna, P., Lenoci, L., Andreucci, D., Gurevich, V.V., Hamm, H.E., DiBenedetto, E. Kinetics of rhodopsin inactivation and its role in regulating recovery and reproducibility of rod photoresponse. PLoS Computational Biology 6, e1001031 (doi: 10.1371/journal.pcbi.1001031) (2010).
Zhuang, T., Vishnivetskiy, S.A., Gurevich, V.V., Sanders, C.R. Elucidation of IP6 and heparin interaction site and conformational changes in arrestin-1 by solution NMR. Biochemistry 49, 10473-10485 (2010).
Ahmed, M.R., Berthet, A., Bychkov, E., Porras, G., Li, Q., Bioulac, B.H., Carl, Y.T., Bloch, B., Kook, S., Aubert, I., Dovero, S., Doudnikoff, E., Gurevich, V.V., Gurevich, E.V., Bezard, E. Lentiviral overexpression of GRK6 alleviates L-DOPA-induced dyskinesia in experimental Parkinson’s disease. Sci Transl Med 2, 28ra28 (2010) http://www.ncbi.nlm.nih.gov/pubmed/20410529
Gurevich, V.V. and Gurevich, E.V. Custom-designed proteins as novel therapeutic tools? The case of arrestins. Expert Rev Mol Med 12, e13, doi: 10.1017/S1462399410001444 (2010) http://www.ncbi.nlm.nih.gov/pubmed/20412604
Shankar, H., Michal, A., Kern, R.C., Kang, D.S., Gurevich, V.V., Benovic, J.L. Non-visual arrestins are constitutively associated with the centrosome and regulate centrosome function. J Biol Chem 285, 8316-29 (2010) http://www.ncbi.nlm.nih.gov/pubmed/20056609
Shen, L., Caruso, G., Bisegna, P., Andreucci, D., Gurevich, V.V., Hamm, H.E., DiBenedetto, E. Dynamics of Mouse Rod Phototransduction and Its Sensitivity to Variation of Key Parameters. IET Syst Biol 4, 12-32 (2010) http://www.ncbi.nlm.nih.gov/pubmed/20001089
Vishnivetskiy, S.A., Francis, D., Van Eps, N., Kim, M., Hanson, S.M., Klug, C.S., Hubbell, W.L, Gurevich, V.V. The role of arrestin a-helix I in receptor binding. J Mol Biol 395, 42-54 (2010) http://www.ncbi.nlm.nih.gov/pubmed/19883657
Gurevich, V.V. and Gurevich, E.V. Phototransduction: inactivation in rods. In: Darlene A. Dartt, editor. Encyclopedia of the Eye, Vol 3. Oxford: Academic Press; pp. 375-380. ISBN-13: 978-0-12-374198-1 (2010).
Gurevich, V.V. and Gurevich, E.V. Phototransduction: inactivation in cones. In: Darlene A. Dartt, editor. Encyclopedia of the Eye, Vol 3. Oxford: Academic Press; pp. 370-374. ISBN-13: 978-0-12-374198-1 (2010)
2009
Song, X., Vishnivetskiy, S.A., Gross, O.P., Emelianoff, K., Mendez, A., Chen, J., Gurevich, E.V., Burns, M.E., Gurevich, V.V. Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation Curr Biol 19, 700-705 (2009) http://www.ncbi.nlm.nih.gov/pubmed/19361994
DiNieri, J., Nemeth, C., Parsegian, A., Carle, T., Gurevich, V.V., Gurevich, E.V., Neve, R., Nestler, E., and Carlezon, W. Altered sensitivity to rewarding and aversive drugs in mice with inducible disruption of CREB function within the nucleus accumbens. J Neurosci 29, 1855-1859 (2009) http://www.ncbi.nlm.nih.gov/pubmed/19211892
Wen, X.-H., Shen, L., Brush, R.S., Michaud, N., Al-Ubaidi, M.R., Gurevich, V.V., Hamm, H.E., Lem, J., DiBenedetto, E., Anderson, R.E., Makino, C.L. Over-expression of rhodopsin alters the structure and photoresponse of rod photoreceptors. Biophys J 96, 939-50 (2009) http://www.ncbi.nlm.nih.gov/pubmed/19186132
Song, X., Coffa, S., Fu, H., Gurevich, V.V. How does arrestin assemble MAP kinases into a signaling complex? J Biol Chem 284, 685-95 (2009) http://www.ncbi.nlm.nih.gov/pubmed/19001375
Lan, H., Teeter, M.M., Gurevich, V.V., and Neve, K.A. An Intracellular Loop 2 Amino Acid Residue Determines Differential Binding of Arrestin to the Dopamine D2 and D3 Receptors. Mol Pharmacol 75,19-26 (2009) http://www.ncbi.nlm.nih.gov/pubmed/18820126
Lan, H., Liu, Y., Bell, M.I., Gurevich, V.V., and Neve, K.A. A Dopamine D2 Receptor Mutant Capable of G Protein-mediated Signaling but Deficient in Arrestin Binding. Mol Pharmacol 75, 113-23 (2009). http://www.ncbi.nlm.nih.gov/pubmed/18809670
Gurevich, E.V. and Gurevich, V.V. Dopamine receptors and treatment of Parkinson’s disease. Chapter 18, pp. 525-585. In: Dopamine Receptors, Second Edition (Neve, K.A., Ed.), ISBN: 978-1-60327-332-9, Humana Press, Totowa, NJ (2009)
2008
Gurevich, V.V. and Gurevich, E.V. GPCR monomers and oligomers: it takes all kinds. Trends Neurosci 31, 74-81 (2008) http://www.ncbi.nlm.nih.gov/pubmed/18199492
Gurevich, V.V. and Gurevich, E.V. How and why do GPCRs dimerize? Trends Pharmacol Sci 29, 234-240 (2008) http://www.ncbi.nlm.nih.gov/pubmed/18384890
Hanson, S.M., Dawson, E.S., Francis, D.J., Van Eps, N., Klug, C.S., Hubbell, W.L., Meiler, J., and Gurevich, V.V. A Model for the Solution Structure of the Rod Arrestin Tetramer. Structure 16, 924-934 (2008). http://www.ncbi.nlm.nih.gov/pubmed/18547524
Gurevich, V.V. Gurevich, E.V. Rich tapestry of GPCR signaling and regulatory mechanisms. Mol Pharmacol 74, 312-316 (2008) http://www.ncbi.nlm.nih.gov/pubmed/18515421
Ahmed, M.R., Gurevich, V.V., Dalby, K.N., Benovic, J.L., and Gurevich, E.V. Haloperidol and clozapine differentially affect the expression of arrestins, receptor kinases, and ERK activation. J Pharmacol Exp Ther 325, 276-83 (2008). http://www.ncbi.nlm.nih.gov/pubmed/18178904
Hanson, S.M., Vishnivetskiy, S.A., Hubbell, W.L., and Gurevich, V.V. The opposing effects of inositol hexakisphosphate (IP6) on rod arrestin and arrestin2 self-association. Biochemistry 47, 1070-5 (2008) http://www.ncbi.nlm.nih.gov/pubmed/18161994
Bisegna, P., Caruso, G., Andreucci, D., Shen, L., Gurevich, V.V., Hamm, H.E., and DiBenedetto, E. Diffusion of the Second Messengers in the Cytoplasm Acts as a Variability Suppressor of the Single Photon Response in Vertebrate Phototransduction. Biophys J, 94, 3363-83 (2008). http://www.ncbi.nlm.nih.gov/pubmed/18400950
Ahmed, M.R., Bychkov, E., Gurevich, V.V., Benovic, J.L., Gurevich, E.V. Altered expression and subcellular distribution of GRK subtypes in the dopamine-depleted rat basal ganglia is not normalized by L-DOPA treatment. J Neurochem 104, 1622-36 (2008). http://www.ncbi.nlm.nih.gov/pubmed/17996024
Gurevich, V.V., Gurevich, E.V., Cleghorn, W.M. Arrestins as multi-functional signaling adaptors. In: Handbook of experimental Pharmacology, vol. 186. Protein-protein interactions as new drug targets (Klussmann, E., and Scott, J., Eds), pp. 15-37. Springer-Verlag, Berlin (2008) http://www.ncbi.nlm.nih.gov/pubmed/18491047
Bychkov ER, Gurevich VV, Joyce JN, Benovic JL, Gurevich EV. Arrestins and two receptor kinases are upregulated in Parkinson’s disease with dementia. Neurobiol Aging 29, 379-96 (2008)
2007
Vishnivetskiy, S.A., Raman, D., Wei, J., Kennedy, M.J., Hurley, J.B., Gurevich, V.V. Regulation of arrestin binding by rhodopsin phosphorylation level. J Biol Chem 282, 32075-83 (2007). http://www.ncbi.nlm.nih.gov/pubmed/17848565
Gurevich, V.V., Hanson, S.M., Gurevich, E.V., Vishnivetskiy, S.A. How Rod Arrestin Achieved Perfection: Regulation of its Availability and Binding Selectivity. In: Signal Transduction in the retina (Kisselev, O., and Fliesler, S.J., Eds), pp 55-88. Methods in Signal Transduction Series, CRC Press, Boca Raton, FL (2007)web pdf/Retina chapter.pdf
Song, X., Gurevich, E.V., and Gurevich, V.V. Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites. J. Neurochem 103, 1053–1062 (2007). http://www.ncbi.nlm.nih.gov/pubmed/17680991
Chan S, Rubin WW, Mendez A, Liu X, Song X, Hanson SM, Craft CM, Gurevich VV, Burns ME, Chen J. Functional comparisons of visual arrestins in rod photoreceptors of transgenic mice. Invest Ophthalmol Vis Sci. 2007 May;48(5):1968-75
Hanson SM, Gurevich EV, Vishnivetskiy SA, Ahmed MR, Song X, Gurevich VV. Each rhodopsin molecule binds its own arrestin. Proc. Natl. Acad. Sci. USA 104, 3125-3128 (2007)
Hanson SM, Cleghorn WM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Nair KS, Slepak VZ, Klug CS, Gurevich VV. Arrestin Mobilizes Signaling Proteins to the Cytoskeleton and Redirects their Activity. J Mol Biol 368, 375-387, 2007
Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV. Structure and function of the visual arrestin oligomer. EMBO J 26, 1726-36, 2007
2006
Wu N, Hanson SM, Francis DJ, Vishnivetskiy SA, Thibonnier M, Klug CS, Shoham M, Gurevich VV. Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins.
J Mol Biol, 364(5),955-63, 2006
Gurevich EV, Gurevich VV. Arrestins: ubiquitous regulators of cellular signaling pathways.
Genome Biol, 7(9), 236, 2006
Song, X., Raman, D., Gurevich, E. V., Vishnivetskiy, S. A., and Gurevich, V. V. Visual and both non-visual arrestins in their “inactive” conformation bind JNK3 and MDM2 and relocalize them from the nucleus to the cytoplasm. J Biol Chem 281 (2006).
Wu, N., Macion-Dazard, R., Nithianantham, S., Xu, Z., Hanson, S.M., Vishnivetskiy, S.A., Gurevich, V.V., Thibonnier, M., and Shoham, M. Soluble mimics of the cytoplasmic face of the human V1-vascular vasopressin receptor bind arrestin2 and calmodulin. Mol Pharmacol 70, 249-258 (2006).
Hanson, SM, Francis, DJ, Vishnivetskiy, SA, Klug, CS, Gurevich, VV. Visual arrestin binding to microtubules involves a distinct conformational change. J Biol Chem, 2006
Hanson, S.M., Francis, D.J., Vishnivetskiy, S.A., Kolobova, E.A., Hubbell, W.L., Klug, C.S., and Gurevich, V.V. Differential interaction of spin labeled arrestin with inactive and active phosphorhodopsin. Proc. Natl. Acad. Sci. USA 103, 4900-4905 (2006).
Gurevich, VV, Gurevich, EV. The structural basis of arrestin-mediated regulation of G-protein-coupled receptors. Pharmacol Ther, 2006
2005 and earlier
Carter, JM, Gurevich, VV, Prossnitz, ER, Engen, JR. Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry. J Mol Biol, 351(4), 865-78, 2005
Hanson, SM, Gurevich, VV. The differential engagement of arrestin surface charges by the variuos functional forms of the receptor. J Biol Chem, 2005
Key, T Alexander, Vines, Charlotte M, Wagener, Brant M, Gurevich, Vsevolod V, Sklar, Larry A, Prossnitz, Eric R. Inhibition of chemoattractant N-formyl peptide receptor trafficking by active arrestins. Traffic, 6(2), 87-99, 2005
Bezard, E., Gross, C.E., Qin, L., Gurevich, V.V., Benovic, J.L., and Gurevich, E.V. L-DOPA reverses the MPTP-induced elevation of the arrestin2 and GRK6 expression and enhanced ERK activation in monkey brain. Neurobiol. Dis. 18, 323-335 (2005).
Macey, TA, Liu, Y, Gurevich, VV, Neve, KA. Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons. J Neurochem, 93(1), 128-34, 2005
Nair, KS, Hanson, SM, Mendez, A, Gurevich, EV, Kennedy, MJ, Shestopalov, VI, Vishnivetskiy, SA, Chen, J, Hurley, JB, Gurevich, VV, Slepak, VZ. Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron, 46(4), 555-67, 2005
Sutton, RB, Vishnivetskiy, SA, Robert, J, Hanson, SM, Raman, D, Knox, BE, Kono, M, Navarro, J, Gurevich, VV. Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J Mol Biol, 354(5), 1069-80, 2005
Zhang, R, Khoo, MS, Wu, Y, Yang, Y, Grueter, CE, Ni, G, Price, EE, Thiel, W, Guatimosim, S, Song, LS, Madu, EC, Shah, AN, Vishnivetskaya, TA, Atkinson, JB, Gurevich, VV, Salama, G, Lederer, WJ, Colbran, RJ, Anderson, ME. Calmodulin kinase II inhibition protects against structural heart disease. Nat Med, 11(4), 409-17, 2005
Guigoni, C., Aubert, I., Qin, L., Gurevich, V.V., Benovic, J.L., Ferry, S., Mach, U., Stark, H., Leriche, L., Hakansson, K., Bioulac, B.H., Gross, C.E., Sokoloff, P., Fisone, G., Gurevich, E.V., Bloch, B., and Bezard, E. Pathogenesis of levodopa-induced dyskinesia: focuse on D1 and D3 dopamine receptors. Parkinsonism Relat Disord 11, S25-S29 (2005).
Gurevich, Eugenia V, Benovic, Jeffrey L, Gurevich, Vsevolod V. Arrestin2 expression selectively increases during neural differentiation. J Neurochem, 91(6), 1404-16, 2004
Macey, Tara A, Gurevich, Vsevolod V, Neve, Kim A. Preferential Interaction between the Dopamine D2 Receptor and Arrestin2 in Neostriatal Neurons. Mol Pharmacol, 66(6), 1635-42, 2004
Nair, K Saidas, Hanson, Susan M, Kennedy, Matthew J, Hurley, James B, Gurevich, Vsevolod V, Slepak, Vladlen Z. Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors. J Biol Chem, 279(39), 41240-8, 2004
Vishnivetskiy, Sergey A., Hosey, M Marlene, Benovic, Jeffrey L., Gurevich, Vsevolod V.. Mapping the arrestin-receptor interface: Structural elements responsible for receptor specificity of arrestin proteins. J Biol Chem, 279, 1262-1268, 2004
Gurevich, Vsevolod V, Gurevich, Eugenia V. The molecular acrobatics of arrestin activation. Trends Pharmacol Sci, 25(2), 105-11, 2004
Shi, M., Bennett, T.A., Cimino, D.F., Maestas, D.C., Foutz, T.D., Gurevich, V.V., Sklar, L.A., Prossnitz, E.R. Functional Capabilities of an N-Formyl Peptide Receptor-G(alpha)(i)(2) Fusion Protein: Assemblies with G Proteins and Arrestins. Biochemistry 42, 7283-7293 (2003).
Gray, J.A., Bhatnagar, A., Gurevich, V.V., and Roth, B.L. The interaction of a constitutively active arrestin with the arrestin-insensitive 5-HT2A receptor induces agonist-independent internalization. Mol. Pharmacol. 63, 961-972 (2003).
Key, T Alexander, Foutz, Terry D, Gurevich, Vsevolod V, Sklar, Larry A, Prossnitz, Eric R. N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity. J Biol Chem, 278(6), 4041-7, 2003
Pan, Ling, Gurevich, Eugenia V, Gurevich, Vsevolod V. The nature of the arrestin x receptor complex determines the ultimate fate of the internalized receptor. J Biol Chem, 278(13), 11623-32, 2003
Raman, Dayanidhi, Osawa, Shoji, Gurevich, Vsevolod V, Weiss, Ellen R. The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding. J Neurochem, 84(5), 1040-50, 2003
Shi, Mei, Bennett, Teresa A, Cimino, Daniel F, Maestas, Diane C, Foutz, Terry D, Gurevich, Vsevolod V, Sklar, Larry A, Prossnitz, Eric R, . Functional capabilities of an N-formyl peptide receptor-G(alpha)(i)(2) fusion protein: assemblies with G proteins and arrestins.. Biochemistry, 42, 7283-93, 2003
Gurevich, Vsevolod V, Gurevich, Eugenia V, . The new face of active receptor bound arrestin attracts new partners.. Structure (Camb), 11, 1037-42, 2003
Celver, Jeremy, Vishnivetskiy, Sergey A, Chavkin, Charles, Gurevich, Vsevolod V. Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J Biol Chem, 277(11), 9043-8, 2002
DeGraff, Jessica L, Gurevich, Vsevolod V, Benovic, Jeffrey L. The third intracellular loop of alpha 2-adrenergic receptors determines subtype specificity of arrestin interaction. J Biol Chem, 277(45), 43247-52, 2002
Gurevich, E V, Benovic, J L, Gurevich, V V. Arrestin2 and arrestin3 are differentially expressed in the rat brain during postnatal development. Neuroscience, 109(3), 421-36, 2002
Lowe, Janet D, Celver, Jeremy P, Gurevich, Vsevolod V, Chavkin, Charles. mu-Opioid receptors desensitize less rapidly than delta-opioid receptors due to less efficient activation of arrestin. J Biol Chem, 277(18), 15729-35, 2002
Mukherjee, Sutapa, Gurevich, Vsevolod V, Preninger, Anita, Hamm, Heidi E, Bader, Marie-France, Fazleabas, Asgerally T, Birnbaumer, Lutz, Hunzicker-Dunn, Mary. Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2. J Biol Chem, 277(20), 17916-27, 2002
Potter, Ross M, Key, T Alexander, Gurevich, Vsevolod V, Sklar, Larry A, Prossnitz, Eric R. Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus. J Biol Chem, 277(11), 8970-8, 2002
Vishnivetskiy, Sergey A, Hirsch, Joel A, Velez, Maria-Gabriela, Gurevich, Yulia V, Gurevich, Vsevolod V. Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge. J Biol Chem, 277(46), 43961-7, 2002
Hunzicker-Dunn, Mary, Gurevich, Vsevolod V, Casanova, James E, Mukherjee, Sutapa. ARF6: a newly appreciated player in G protein-coupled receptor desensitization. FEBS Lett, 521(1-3), 3-8, 2002
Bennett, T A, Foutz, T D, Gurevich, V V, Sklar, L A, Prossnitz, E R. Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding. J Biol Chem, 276(52), 49195-203, 2001
Bennett, T A, Key, T A, Gurevich, V V, Neubig, R, Prossnitz, E R, Sklar, L A. Real-time analysis of G protein-coupled receptor reconstitution in a solubilized system. J Biol Chem, 276(25), 22453-60, 2001
Celver, J P, Lowe, J, Kovoor, A, Gurevich, V V, Chavkin, C. Threonine 180 is required for G-protein-coupled receptor kinase 3- and beta-arrestin 2-mediated desensitization of the mu-opioid receptor in Xenopus oocytes. J Biol Chem, 276(7), 4894-900, 2001
Han, M, Gurevich, V V, Vishnivetskiy, S A, Sigler, P B, Schubert, C. Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. Structure (Camb), 9(9), 869-80, 2001
Key, T A, Bennett, T A, Foutz, T D, Gurevich, V V, Sklar, L A, Prossnitz, E R. Regulation of formyl peptide receptor agonist affinity by reconstitution with arrestins and heterotrimeric G proteins. J Biol Chem, 276(52), 49204-12, 2001
Lee, K B, Ptasienski, J A, Pals-Rylaarsdam, R, Gurevich, V V, Hosey, M M. Arrestin binding to the M(2) muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor. J Biol Chem, 275(13), 9284-9, 2000
Mukherjee, S, Gurevich, V V, Jones, J C, Casanova, J E, Frank, S R, Maizels, E T, Bader, M F, Kahn, R A, Palczewski, K, Aktories, K, Hunzicker-Dunn, M. The ADP ribosylation factor nucleotide exchange factor ARNO promotes beta-arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization. Proc Natl Acad Sci U S A, 97(11), 5901-6, 2000
Mushegian, A R, Vishnivetskiy, S A, Gurevich, V V. Conserved phosphoprotein interaction motif is functionally interchangeable between ataxin-7 and arrestins. Biochemistry, 39(23), 6809-13, 2000
Smith, W C, Gurevich, E V, Dugger, D R, Vishnivetskiy, S A, Shelamer, C L, McDowell, J H, Gurevich, V V. Cloning and functional characterization of salamander rod and cone arrestins. Invest Ophthalmol Vis Sci, 41(9), 2445-55, 2000
Vishnivetskiy, S A, Schubert, C, Climaco, G C, Gurevich, Y V, Velez, M G, Gurevich, V V. An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation. J Biol Chem, 275(52), 41049-57, 2000
Gurevich, V V, Benovic, J L. Arrestin: mutagenesis, expression, purification, and functional characterization. Methods Enzymol, 315, 422-37, 2000
Hirsch, J A, Schubert, C, Gurevich, V V, Sigler, P B. The 2.8 A crystal structure of visual arrestin: a model for arrestin’s regulation. Cell, 97(2), 257-69, 1999
Hosey, M M, Pals-Rylaarsdam, R, Lee, K B, Roseberry, A G, Benovic, J L, Gurevich, V V, Bünemann, M. Molecular events associated with the regulation of signaling by M2 muscarinic receptors. Life Sci, 64(6-7), 363-8, 1999
Kovoor, A, Celver, J, Abdryashitov, R I, Chavkin, C, Gurevich, V V. Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells. J Biol Chem, 274(11), 6831-4, 1999
Mukherjee, S, Palczewski, K, Gurevich, V V, Hunzicker-Dunn, M. beta-arrestin-dependent desensitization of luteinizing hormone/choriogonadotropin receptor is prevented by a synthetic peptide corresponding to the third intracellular loop of the receptor. J Biol Chem, 274(19), 12984-9, 1999
Schubert, C, Hirsch, J A, Gurevich, V V, Engelman, D M, Sigler, P B, Fleming, K G. Visual arrestin activity may be regulated by self-association. J Biol Chem, 274(30), 21186-90, 1999
Vishnivetskiy, S A, Paz, C L, Schubert, C, Hirsch, J A, Sigler, P B, Gurevich, V V. How does arrestin respond to the phosphorylated state of rhodopsin?. J Biol Chem, 274(17), 11451-4, 1999
Mukherjee, S., Palczewski, K., Gurevich, V.V., Benovic, J.L., Banga, J.P., and Hunzicker-Dunn, M. A direct role for arrestins in desensitization of luteinizing hormone/choriogonatropin receptor in porcine ovarian follicular membranes. Proc. Natl. Acad. Sci. USA, 96, 493-498 (1999).
Gelber, E.I., Kroeze, W.K., Willins, D.L., Gray, J.A., Sinar, C.A., Hyde, E. G., Gurevich, V.V., Benovic, J.L., and Roth, B.L. Structure and function of the third intracellular loop of the 5-hydroxytryptamine-2A receptor: the third intracellular loop is alpha-helical and binds purified arrestins. J. Neurochem. 72, 2206-2214 (1999).
Gurevich, V. V., Orsini, M.J., and Benovic, J.L. Characterization of arrestin expression and function. In: Receptor Biochemistry and Methodology, Vol. IV, 157-178 (1999).
Goodman, O B, Krupnick, J G, Santini, F, Gurevich, V V, Penn, R B, Gagnon, A W, Keen, J H, Benovic, J L. Role of arrestins in G-protein-coupled receptor endocytosis. Adv Pharmacol, 42, 429-33, 1998
Gurevich, V V. The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms. J Biol Chem, 273(25), 15501-6, 1998
Goodman, O B, Krupnick, J G, Gurevich, V V, Benovic, J L, Keen, J H. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J Biol Chem, 272(23), 15017-22, 1997
Gray-Keller, M P, Detwiler, P B, Benovic, J L, Gurevich, V V. Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion. Biochemistry, 36(23), 7058-63, 1997
Gurevich, V V, Pals-Rylaarsdam, R, Benovic, J L, Hosey, M M, Onorato, J J. Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. J Biol Chem, 272(46), 28849-52, 1997
Krupnick, J G, Gurevich, V V, Benovic, J L. Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. J Biol Chem, 272(29), 18125-31, 1997
Pals-Rylaarsdam, R, Gurevich, V V, Lee, K B, Ptasienski, J A, Benovic, J L, Hosey, M M. Internalization of the m2 muscarinic acetylcholine receptor. Arrestin-independent and -dependent pathways. J Biol Chem, 272(38), 23682-9, 1997
Gurevich, V.V., and Benovic, J.L. Mechanism of phosphorylation-recognition by visual arrestin and its role in arrestin transition into high-affinity binding state. Mol. Pharmacol. 51, 161-169 (1997).
Goodman, O B, Krupnick, J G, Santini, F, Gurevich, V V, Penn, R B, Gagnon, A W, Keen, J H, Benovic, J L. Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature, 383(6599), 447-50, 1996
Gurevich, V.V. Use of bacteriophage RNA polymerase in RNA synthesis. In: Methods in Enzymology , v. 275 (Kuo, L.C., Olsen, D.B., and Carroll, S.S., Eds.), 382-397 (1996).
Gurevich, V V, Benovic, J L. Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin. J Biol Chem, 270(11), 6010-6, 1995
Gurevich, V V, Dion, S B, Onorato, J J, Ptasienski, J, Kim, C M, Sterne-Marr, R, Hosey, M M, Benovic, J L. Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors. J Biol Chem, 270(2), 720-31, 1995
Pokrovskaya, I.D., and Gurevich, V.V. In vitro transcription: preparative yields in analytical scale reactions. Anal. Biochem. 220, 420-423 (1994).
Kunapuli, P., Gurevich, V.V., and Benovic, J.L. Phospholipid-stimulated autophosphorylation activates the G protein-coupled receptor kinase GRK5. J.Biol.Chem. 269, 10209-10212 (1994).
Gurevich, V.V., Chen, C.-Y., Kim, C.M., and Benovic, J.L. Visual arrestin binding to rhodopsin: Intramolecular interaction between the basic N-terminus and acidic C-terminus of arrestin may regulate binding selectivity. J.Biol.Chem. 269, 8721-8727 (1994).
Krupnick, J.G., Gurevich, V.V., Schepers, T., Hamm, H.E., and Benovic, J.L. Arrestin-rhodopsin interaction: Multi-site binding delineated by peptide inhibition. J.Biol.Chem. 269,3226-3232 (1994).
Gurevich, V V, Benovic, J L. Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J Biol Chem, 268(16), 11628-38, 1993
Sterne-Marr, R, Gurevich, V V, Goldsmith, P, Bodine, R C, Sanders, C, Donoso, L A, Benovic, J L. Polypeptide variants of beta-arrestin and arrestin3. J Biol Chem, 268(21), 15640-8, 1993
Gurevich, V.V., and Benovic, J.L. Visual arrestin interaction with rhodopsin: Sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin. J.Biol.Chem. 268, 11628-11638 (1993).
Gurevich, V.V., and Benovic, J.L. Cell-free expression of visual arrestin: Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction. J.Biol.Chem. 267, 21919-21923 (1992).
Gurevich, V.V., Zozulya, S.A., Pokrovskaya, I.D., and Obukhova, T.A. Preparative in vitro mRNA synthesis using SP6 and T7 RNA polymerases. Anal. Biochem. 195, 207-213 (1991).