Nicole Perry
Graduate Sudent, Pharmacology
Nicki received her B.S./B.A. in Biology and Chemistry at Wittenberg University, Springfield, OH
Research Description
Nicki was under the co-mentorship of Dr. Gurevich and Dr. Iverson, whose labs she officially joined in April 2015. Her chosen thesis research, which is to elucidate arrestin interactions with effectors, is based on evidence from both labs and current publications in the field. As a member of two labs, Nicki was presented with the unique opportunity to approach her scientific questions from two angles: biochemical assays, which allow her to conduct studies of arrestin function, and X-ray crystallography, which she uses to determine different arrestin complex structures. This arrangement enabled her to develop novel functional experiments with the help of solved crystal structures, a process that usually requires extensive collaboration. It also exposed her to a wide variety of experimental techniques, which range from basic molecular and cell biology to advanced instrumental study.
Nicki defended her thesis on March 4, 2019. She moved as a post-doc to Columbia University in June 2019. Married name: Perry-Hauser.
Funding
Publications from the lab (one more is in preparation)
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).
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).
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).
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).
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)
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, vol. 1957, 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 (2019).
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).
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 (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).
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).
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).
Previous Publication
Xu T, Perry N, Chauhan A, Sayler G, Ripp S. 2014. Microbial indicators for monitoring pollution and bioremediation p.115-132. In Das S (ed.), Microbial Biodegradation and Bioremediation. Elsevier, New York, NY.