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Faiza Baameur, PhD

Post-doctoral fellow, Pharmacology

1993 BS in Chemistry, University of Oran, Algeria
2000 MS in Physical Chemistry, University of Oran, Algeria. Mentor: Dr. Abdelghani Krallafa
2009 PhD in Pharmacology, University of Texas Health Science Center at Houston. Mentor: Dr. Richard Clark

Research Description

Faiza worked in the lab from January 2012 to December 2013. She was addressing the functions of different arrestin proteins in cells and live animals. She was studying biochemical mechanism of arrestin-3-dependent scaffolding of ASK1-MKK4-JNK3 MAP kinase cascade that promotes cell death. Harnessing this modality of arrestin function to reduce JNK signaling holds promise as a novel therapeutic approach to neurodegenerative diseases, whereas using this information to enhance pro-apoptotic JNK signaling paves the way to novel treatments of cancer. Faiza also made transgenic mice expressing constitutively monomeric visual arrestin-1 to elucidate the biological role of arrestin-1 self-association in vivo. Arrestin-1 is the only signaling protein in photoreceptors that is stored in inactive oligomeric form in several mammalian species, including mice and humans. Although several ideas have been proposed, we do not really understand the purpose of this mechanism.

Publications from the lab

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,  in press (2015). doi: 10.7554/eLife.05981.

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).

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., 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).

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).


Previous publications

Baameur F, Hammitt RA, Friedman J, McMurray JS, Clark RB. Evaluation of the Biochemical and Cellular Specificity of Peptide Inhibitors of G Protein-Coupled Receptor Kinases. Int J Pept Res Ther 2013

Baameur F, Krallafa A, Aourag H, and Khelifa K. Molecular Dynamics simulation of solid C60 under progressively raised pressure. Physica Status solidi review: Phys. Stat. Sol. (b) 220, III (2000).

Tran TM, Friedman J, Qunaibi E, Baameur F, Moore RH, Clark RB. Characterization of agonist stimulation of cAMP-dependent protein kinase and G protein-coupled receptor kinase phosphorylation of the beta2-adrenergic receptor using phosphoserine-specific antibodies. Mol Pharmacol. 2004 Jan;65(1):196-206.

Tran TM, Friedman J, Baameur F, Knoll BJ, Moore RH, Clark RB. Characterization of beta2-adrenergic receptor dephosphorylation: Comparison with the rate of resensitization. Mol Pharmacol. 2007 Jan;71(1):47-60.

Baameur F, Morgan DH, Yao H, Tran TM, Hammitt RA, Sabui S, McMurray JS, Lichtarge O, Clark RB. Role for the regulator of G-protein signaling homology domain of G protein-coupled receptor kinases 5 and 6 in beta 2-adrenergic receptor and rhodopsin phosphorylation. Mol Pharmacol. 2010 Mar;77(3):405-15. Epub 2009 Dec 28.

Efendiev R, Samelson BK, Nguyen BT, Phatarpekar PV, Baameur F, Scott JD, Dessauer CW. AKAP79 interacts with multiple adenylyl cyclase (AC) isoforms and scaffolds AC5 and -6 to alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate (AMPA) receptors. J Biol Chem. 2010 May 7;285(19):14450-8.