Vanderbilt University School of Medicine

Gurevich, Vsevolod V. , Ph.D.
Professor of Pharmacology

Lab Url: https://medschool.vanderbilt.edu/gurevich-lab/

Phone Number: (615) 322-7070

Email Address:vsevolod.gurevich@vanderbilt.edu

Gurevich, Vsevolod's picture

Office Address   Mailing Address

417D Preston Research Building

417D PRB 37232-6600


Research Keywords
Arrestins Structure-function G protein-coupled receptors Vision Signal transduction Trafficking Neurodevelopment Transgenic animal models Cell survival,Apoptosis,Biochemistry,Molecular medicine,Neuroscience,Pharmacology,Phosphorylation,Protein Structure,Receptor,Signal transduction,Structural Biology,Vision

Research Description
We are interested in structure, function, and biology of arrestin proteins. Arrestins bind activated phosphorylated G protein-coupled receptors (GPCRs), thereby shutting down their signaling via G proteins (desensitization), targeting receptors for internalization. Free and receptor-bound arrestins are multi-functional signaling adapters, interacting with more than 20 signaling proteins, many of which play key role in "life-or-death" decisions in the cell. We want to understand the molecular mechanisms that arrestins use to "decide" when to bind particular interaction partners and when to dissociate. We have mapped receptor-arrestin interaction interface fairly well and we want to elucidate arrestin binding sites for its other interaction partners with the same precision. We intend to use this information to construct "custom-designed" arrestins that link the receptor of interest to the signaling pathway of our choosing. These tools will allow us to tell the cell what to do and when to do it. For example, "biased" arrestins can enhance pro-survival signaling, preventing cell death characteristic for neurodegenerative diseases (such as Alzheimer's, Parkinson's, or retinal degeneration), or tip the balance toward cell death, which would be useful to prevent uncontrolled proliferation characteristic for cancer.
The solution of the crystal structure of three arrestin proteins and elucidation of the mechanism of arrestin phosphate sensor action allowed us to construct arrestin mutants that bind the active form of their cognate GPCRs regardless of receptor phosphorylation. These "super-arrestins" may prove useful for gene therapy of disorders associated with excessive signaling by various GPCRs that range from night blindness and retinal degeneration to several forms of cancer. We are testing whether transgenic expression of phosphorylation-independent mutants of visual arrestin prevents retinal degeneration in several mouse models.
We believe that the combination of different approaches ranging from hard-core biochemical and biophysical methods and X-ray crystallography to cell culture and transgenic animals is necessary to answer biologically relevant questions concerning various facets of arrestin function and to create novel therapeutic tools based on this information.

Publications
Gurevich, VV, Gurevich, EV. Structural determinants of arrestin functions. Prog Mol Biol Transl Sci, 118, 57-92, 2013.

Song, X, Seo, J, Baameur, F, Vishnivetskiy, SA, Chen, Q, Kook, S, Kim, M, Brooks, EK, Altenbach, C, Hong, Y, Hanson, SM, Palazzo, MC, Chen, J, Hubbell, WL, Gurevich, EV, Gurevich, VV. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant. Cell Signal, 25(12), 2613-2624, 2013.

Vishnivetskiy, SA, Baameur, F, Findley, KR, Gurevich, VV. Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. J Biol Chem, 288(17), 11741-50, 2013.

Vishnivetskiy, SA, Chen, Q, Palazzo, MC, Brooks, EK, Altenbach, C, Iverson, TM, Hubbell, WL, Gurevich, VV. Engineering visual arrestin-1 with special functional characteristics. J Biol Chem, 288(5), 3394-405, 2013.

Vishnivetskiy, SA, Ostermaier, MK, Singhal, A, Panneels, V, Homan, KT, Glukhova, A, Sligar, SG, Tesmer, JJ, Schertler, GF, Standfuss, J, Gurevich, VV. Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding. Cell Signal, 25(11), 2155-62, 2013.

Zhan, X, Kaoud, TS, Kook, S, Dalby, KN, Gurevich, VV. JNK3 binding to arrestin-3 differentially affects the recruitment of upstream MAP kinase kinases. J Biol Chem, , , 2013.

Zhuang, T, Chen, Q, Cho, MK, Vishnivetskiy, SA, Iverson, TM, Gurevich, VV, Sanders, CR. Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci U S A, 110(3), 942-7, 2013.

Aguila, B, Coulbault, L, Davis, A, Marie, N, Hasbi, A, Le bras, F, T??th, G, Borsodi, A, Gurevich, VV, Jauzac, P, Allouche, S. ??arrestin1-biased agonism at human I'-opioid receptor by peptidic and alkaloid ligands. Cell Signal, 24(3), 699-707, 2012. PMCID:3236217

Breitman, M, Kook, S, Gimenez, LE, Lizama, BN, Palazzo, MC, Gurevich, EV, Gurevich, VV. Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant. J Biol Chem, 287(23), 19653-64, 2012.

Gimenez, LE, Kook, S, Vishnivetskiy, SA, Ahmed, MR, Gurevich, EV, Gurevich, VV. Role of Receptor-attached Phosphates in Binding of Visual and Non-visual Arrestins to G Protein-coupled Receptors. J Biol Chem, 287(12), 9028-40, 2012.

Gimenez, LE, Vishnivetskiy, SA, Baameur, F, Gurevich, VV. Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins. J Biol Chem, 287(35), 29495-505, 2012.

Gurevich, VV, Gurevich, EV. Synthetic biology with surgical precision: targeted reengineering of signaling proteins. Cell Signal, 24(10), 1899-908, 2012.

Mushegian, A, Gurevich, VV, Gurevich, EV. The Origin and Evolution of G Protein-Coupled Receptor Kinases. PLoS One, 7(3), e33806, 2012.

Ahmed, MR, Zhan, X, Song, X, Kook, S, Gurevich, VV, Gurevich, EV. Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination. Biochemistry, 50(18), 3749-63, 2011. PMCID:3144249

Bayburt, TH, Vishnivetskiy, SA, McLean, MA, Morizumi, T, Huang, CC, Tesmer, JJ, Ernst, OP, Sligar, SG, Gurevich, VV. Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J Biol Chem, 286(2), 1420-8, 2011. PMCID:3002991

Bychkov, ER, Ahmed, MR, Gurevich, VV, Benovic, JL, Gurevich, EV. Reduced expression of G protein-coupled receptor kinases in schizophrenia but not in schizoaffective disorder. Neurobiol Dis, 44(2), 248-58, 2011. PMCID:3144249

Caruso, G, Bisegna, P, Andreucci, D, Lenoci, L, Gurevich, VV, Hamm, HE, DiBenedetto, E. Identification of key factors that reduce the variability of the single photon response. Proc Natl Acad Sci U S A, 108(19), 7804-7, 2011. PMCID:3144249

Cleghorn, WM, Tsakem, EL, Song, X, Vishnivetskiy, SA, Seo, J, Chen, J, Gurevich, EV, Gurevich, VV. Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery. PLoS One, 6(7), e22797, 2011. PMCID:3144249

Coffa, S, Breitman, M, Hanson, SM, Callaway, K, Kook, S, Dalby, KN, Gurevich, VV. The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation. PLoS One, 6(12), e28723, 2011. PMCID:3236217

Coffa, S, Breitman, M, Spiller, BW, Gurevich, VV. A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding. Biochemistry, 50(32), 6951-8, 2011. PMCID:3144249

Gurevich, EV, Tesmer, JJ, Mushegian, A, Gurevich, VV. G protein-coupled receptor kinases: More than just kinases and not only for GPCRs. Pharmacol Ther, , , 2011.

Gurevich, VV, Hanson, SM, Song, X, Vishnivetskiy, SA, Gurevich, EV. The functional cycle of visual arrestins in photoreceptor cells. Prog Retin Eye Res, 30(6), 405-30, 2011.

Kim, M, Hanson, SM, Vishnivetskiy, SA, Song, X, Cleghorn, WM, Hubbell, WL, Gurevich, VV. Robust self-association is a common feature of Mammalian visual arrestin-1. Biochemistry, 50(12), 2235-42, 2011.

Seo, J, Tsakem, EL, Breitman, M, Gurevich, VV. Identification of arrestin-3-specific residues necessary for JNK3 kinase activation. J Biol Chem, 286(32), 27894-901, 2011. PMCID:3144249

Song, X, Vishnivetskiy, SA, Seo, J, Chen, J, Gurevich, EV, Gurevich, VV. Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health. Neuroscience, 174, 37-49, 2011. PMCID:3002991

Vishnivetskiy, SA, Gimenez, LE, Francis, DJ, Hanson, SM, Hubbell, WL, Klug, CS, Gurevich, VV. Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. J Biol Chem, 286(27), 24288-99, 2011. PMCID:3144249

Zhan, X, Gimenez, LE, Gurevich, VV, Spiller, BW. Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol, 406(3), 467-78, 2011.

Zhan, X, Kaoud, TS, Dalby, KN, Gurevich, VV. Non-visual arrestins function as simple scaffolds assembling the MKK4-JNK3a2 signaling complex. Biochemistry, , , 2011.

Ahmed, MR, Berthet, A, Bychkov, E, Porras, G, Li, Q, Bioulac, BH, Carl, YT, Bloch, B, Kook, S, Aubert, I, Dovero, S, Doudnikoff, E, Gurevich, VV, Gurevich, EV, Bezard, E. Lentiviral overexpression of GRK6 alleviates L-dopa-induced dyskinesia in experimental Parkinson''s disease. Sci Transl Med, 2(28), 28ra28, 2010. PMCID:2933751

Caruso, G, Bisegna, P, Lenoci, L, Andreucci, D, Gurevich, VV, Hamm, HE, DiBenedetto, E. Kinetics of rhodopsin deactivation and its role in regulating recovery and reproducibility of rod photoresponse. PLoS Comput Biol, 6(12), e1001031, 2010. PMCID:3002991

Gurevich, VV, Gurevich, EV. Custom-designed proteins as novel therapeutic tools? The case of arrestins. Expert Rev Mol Med, 12, e13, 2010. PMCID:2933791

Shankar, H, Michal, A, Kern, RC, Kang, DS, Gurevich, VV, Benovic, JL. Non-visual arrestins are constitutively associated with the centrosome and regulate centrosome function. J Biol Chem, 285(11), 8316-29, 2010. PMCID:2832982

Shen, L, Caruso, G, Bisegna, P, Andreucci, D, Gurevich, VV, Hamm, HE, DiBenedetto, E. Dynamics of mouse rod phototransduction and its sensitivity to variation of key parameters. IET Syst Biol, 4(1), 12-32, 2010. PMCID:2832982

Vishnivetskiy, SA, Francis, D, Van Eps, N, Kim, M, Hanson, SM, Klug, CS, Hubbell, WL, Gurevich, VV. The role of arrestin alpha-helix I in receptor binding. J Mol Biol, 395(1), 42-54, 2010. PMCID:2787876

Walther, C, Nagel, S, Gimenez, LE, M??rl, K, Gurevich, VV, Beck-Sickinger, AG. Ligand-induced internalization and recycling of the human neuropeptide Y2 receptor is regulated by its carboxyl-terminal tail. J Biol Chem, 285(53), 41578-90, 2010. PMCID:3002991

Zhuang, T, Vishnivetskiy, SA, Gurevich, VV, Sanders, CR. Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance. Biochemistry, 49(49), 10473-85, 2010. PMCID:3002991

Dinieri, JA, Nemeth, CL, Parsegian, A, Carle, T, Gurevich, VV, Gurevich, E, Neve, RL, Nestler, EJ, Carlezon, WA. Altered sensitivity to rewarding and aversive drugs in mice with inducible disruption of cAMP response element-binding protein function within the nucleus accumbens. J Neurosci, 29(6), 1855-9, 2009. PMCID:2666984

Lan, H, Liu, Y, Bell, MI, Gurevich, VV, Neve, KA. A dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin binding. Mol Pharmacol, 75(1), 113-23, 2009. PMCID:2606918

Lan, H, Teeter, MM, Gurevich, VV, Neve, KA. An intracellular loop 2 amino acid residue determines differential binding of arrestin to the dopamine D2 and D3 receptors. Mol Pharmacol, 75(1), 19-26, 2009. PMCID:2606909

Song, X, Coffa, S, Fu, H, Gurevich, VV. How Does Arrestin Assemble MAPKs into a Signaling Complex. J Biol Chem, 284(1), 685-95, 2009. PMCID:2610502

Song, X, Vishnivetskiy, SA, Gross, OP, Emelianoff, K, Mendez, A, Chen, J, Gurevich, EV, Burns, ME, Gurevich, VV. Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation. Curr Biol, 19(8), 700-5, 2009.

Wen XH, Shen L, Brush RS, Michaud N, Al-Ubaidi MR, Gurevich VV, Hamm HE, Lem J, Dibenedetto E, Anderson RE, Makino CL. Overexpression of rhodopsin alters the structure and photoresponse of rod photoreceptors. Biophys J, 96(3), 93-50, 2009.

Wen, XH, Shen, L, Brush, RS, Michaud, N, Al-Ubaidi, MR, Gurevich, VV, Hamm, HE, Lem, J, Dibenedetto, E, Anderson, RE, Makino, CL. Overexpression of rhodopsin alters the structure and photoresponse of rod photoreceptors. Biophys J, 96(3), 939-50, 2009. PMCID:2716671

Ahmed, MR, Gurevich, VV, Dalby, KN, Benovic, JL, Gurevich, EV. Haloperidol and clozapine differentially affect the expression of arrestins, receptor kinases, and extracellular signal-regulated kinase activation. J Pharmacol Exp Ther, 325(1), 276-83, 2008. PMCID:2629350

Bisegna, P, Caruso, G, Andreucci, D, Shen, L, Gurevich, VV, Hamm, HE, 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(9), 3363-83, 2008. PMCID:2292384

Gurevich, VV, Gurevich, EV. Rich tapestry of G protein-coupled receptor signaling and regulatory mechanisms. Mol Pharmacol, 74(2), 312-6, 2008.

Gurevich, VV, Gurevich, EV. How and why do GPCRs dimerize. Trends Pharmacol Sci, 29(5), 234-40, 2008. PMCID:2652501

Gurevich, VV, Gurevich, EV. GPCR monomers and oligomers: it takes all kinds. Trends Neurosci, 31(2), 74-81, 2008. PMCID:2366802

Gurevich, VV, Gurevich, EV, Cleghorn, WM. Arrestins as multi-functional signaling adaptors. Handb Exp Pharmacol, (186), 15-37, 2008.

Hanson, SM, Dawson, ES, Francis, DJ, Van Eps, N, Klug, CS, Hubbell, WL, Meiler, J, Gurevich, VV. A model for the solution structure of the rod arrestin tetramer. Structure, 16(6), 924-34, 2008. PMCID:2464289

Hanson, SM, Vishnivetskiy, SA, Hubbell, WL, Gurevich, VV. Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association. Biochemistry, 47(3), 1070-5, 2008. PMCID:2562240

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(2), 375-87, 2007. PMCID:1904837

Hanson, SM, Gurevich, EV, Vishnivetskiy, SA, Ahmed, MR, Song, X, Gurevich, VV. Each rhodopsin molecule binds its own arrestin. Proc Natl Acad Sci U S A, 104(9), 3125-8, 2007. PMCID:1805568

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(6), 1726-36, 2007. PMCID:1829381

Song, X, Gurevich, EV, Gurevich, VV. Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites. J Neurochem, 103(3), 1053-62, 2007. PMCID:2430867

Vishnivetskiy, SA, Raman, D, Wei, J, Kennedy, MJ, Hurley, JB, Gurevich, VV. Regulation of arrestin binding by rhodopsin phosphorylation level. J Biol Chem, 282(44), 32075-83, 2007. PMCID:2638115

Gurevich, EV, Gurevich, VV. Arrestins: ubiquitous regulators of cellular signaling pathways. Genome Biol, 7(9), 236, 2006. PMCID:1794542

Gurevich, VV, Gurevich, EV. The structural basis of arrestin-mediated regulation of G-protein-coupled receptors. Pharmacol Ther, 110, 465-502, 2006. PMCID:2562282

Hanson, SM, Francis, DJ, Vishnivetskiy, SA, Klug, CS, Gurevich, VV. Visual arrestin binding to microtubules involves a distinct conformational change. J Biol Chem, , , 2006. PMCID:2430877

Hanson, SM, Francis, DJ, Vishnivetskiy, SA, Kolobova, EA, Hubbell, WL, Klug, CS, Gurevich, VV. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc Natl Acad Sci U S A, 103(13), 4900-5, 2006. PMCID:1458767

Song, X, Raman, D, Gurevich, EV, Vishnivetskiy, SA, Gurevich, VV. 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(30), 21491-9, 2006. PMCID:2430869

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. PMCID:1783800

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. PMCID:2440687

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. PMCID:2752952

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.

Gurevich, Eugenia V, Benovic, Jeffrey L, Gurevich, Vsevolod V. Arrestin2 expression selectively increases during neural differentiation. J Neurochem, 91(6), 1404-16, 2004.

Gurevich, Vsevolod V, Gurevich, Eugenia V. The molecular acrobatics of arrestin activation. Trends Pharmacol Sci, 25(2), 105-11, 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 new face of active receptor bound arrestin attracts new partners.. Structure (Camb), 11, 1037-42, 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.

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.

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.

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.

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.

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. PMCID:18531

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.

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.

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.

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.

Gurevich, VV, Pals-Rylaarsdam, R, Benovic, JL, Hosey, MM, Onorato, JJ. Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. J Biol Chem, 272(46), 28849-52, 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, VV, Dion, SB, Onorato, JJ, Ptasienski, J, Kim, CM, Sterne-Marr, R, Hosey, MM, Benovic, JL. 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.

Gurevich, VV, Benovic, JL. Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J Biol Chem, 268(16), 11628-38, 1993.


Postdoctoral Position Available
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Postdoctoral Position Details
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Updated Date
11/05/2013



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