References

1. Ovchinnikov, Y.A. Rhodopsin and bacteriorhodopsin: Structure-function relationship. FEBS Lett. 1982, 148, 179–191.
2. Dixon, R.A.; Kobilka, B.K.; Strader, D.J.; Benovic, J.L.; Dohlman, H.G.; Frielle, T.; Bolanowski, M.A.; Bennett, C.D.; Rands, E.; Diehl, R.E.; et al. Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin. Nature 1986, 321, 75–79.
3. Fredriksson, R.; Lagerstrom, M.C.; Lundin, L.G.; Schioth, H.B. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 2003, 63, 1256–1272.
4. Farrens, D.L.; Altenbach, C.; Yang, K.; Hubbell, W.L.; Khorana, H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 1996, 274, 768–770.
5. Kuhn, H. Light-regulated binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes. Biochemistry 1978, 17, 4389–4395.
6. Gurevich, V.V.; Gurevich, E.V. The molecular acrobatics of arrestin activation. Trends Pharmacol. Sci. 2004, 25, 105–111.
7. Rasmussen, S.G.; Choi, H.J.; Rosenbaum, D.M.; Kobilka, T.S.; Thian, F.S.; Edwards, P.C.; Burghammer, M.; Ratnala, V.R.; Sanishvili, R.; Fischetti, R.F.; et al. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 2007, 450, 383–387.
8. Kang, Y.; Zhou, X.E.; Gao, X.; He, Y.; Liu, W.; Ishchenko, A.; Barty, A.; White, T.A.; Yefanov, O.; Han, G.W.; et al. Crystal structure of rhodopsin bound to arrestin determined by femtosecond X-ray laser. Nature 2015, 523, 561–567.
9. Komolov, K.E.; Du, Y.; Duc, N.M.; Betz, R.M.; Rodrigues, J.P.G.L.M.; Leib, R.D.; Patra, D.; Skiniotis, G.; Adams, C.M.; Dror, R.O.; et al. Structural and Functional Analysis of a β2-Adrenergic Receptor Complex with GRK5. Cell 2017, 169, 407–421.
10. Manglik, A.; Kim, T.H.; Masureel, M.; Altenbach, C.; Yang, Z.; Hilger, D.; Lerch, M.T.; Kobilka, T.S.; Thian, F.S.; Hubbell, W.L.; et al. Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling. Cell 2015, 161, 1101–1111.
11. Tobin, A.B.; Butcher, A.J.; Kong, K.C. Location, location, location...site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling. Trends Pharmacol. Sci. 2008, 29, 413–420.
12. Nobles, K.N.; Xiao, K.; Ahn, S.; Shukla, A.K.; Lam, C.M.; Rajagopal, S.; Strachan, R.T.; Huang, T.Y.; Bressler, E.A.; Hara, M.R.; et al. Distinct phosphorylation sites on the β2-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. Sci. Signal. 2011, 4, ra51.
13. Carman, C.V.; Benovic, J.L. G-protein-coupled receptors: Turn-ons and turn-offs. Curr. Opin. Neurobiol. 1998, 8, 335–344.
14. Samama, P.; Cotecchia, S.; Costa, T.; Lefkowitz, R.J. A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 1993, 268, 4625–4636.
15. Yao, X.J.; Vélez Ruiz, G.; Whorton, M.R.; Rasmussen, S.G.; DeVree, B.T.; Deupi, X.; Sunahara, R.K.; Kobilka, B. The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex. Proc. Natl. Acad. Sci. USA 2009, 106, 9501–9506.
16. Kenakin, T.; Christopoulos, A. Signalling bias in new drug discovery: Detection, quantification and therapeutic impact. Nat. Rev. Drug Discov. 2013, 12, 205–216.
17. Rosenbaum, D.M.; Zhang, C.; Lyons, J.A.; Holl, R.; Aragao, D.; Arlow, D.H.; Rasmussen, S.G.; Choi, H.J.; Devree, B.T.; Sunahara, R.K.; et al. Structure and function of an irreversible agonist-β2 adrenoceptor complex. Nature 2011, 469, 236–240.
18. Rasmussen, S.G.; Choi, H.J.; Fung, J.J.; Pardon, E.; Casarosa, P.; Chae, P.S.; Devree, B.T.; Rosenbaum, D.M.; Thian, F.S.; Kobilka, T.S.; et al. Structure of a nanobody-stabilized active state of the β2 adrenoceptor. Nature 2011, 469, 175–180.
19. Wisler, J.W.; Xiao, K.; Thomsen, A.R.; Lefkowitz, R.J. Recent developments in biased agonism. Curr. Opin. Cell Biol. 2014, 27, 18–24.
20. Urs, N.M.; Peterson, S.M.; Caron, M.G. New Concepts in Dopamine D2 Receptor Biased Signaling and Implications for Schizophrenia Therapy. Biol. Psychiatry 2017, 81, 78–85.
21. Costa-Neto, C.M.; Parreiras-E-Silva, L.T.; Bouvier, M. A Pluridimensional View of Biased Agonism. Mol. Pharmacol. 2016, 90, 587–595.
22. Carpenter, B.; Nehmé, R.; Warne, T.; Leslie, A.G.; Tate, C.G. Structure of the adenosine A2A receptor bound to an engineered G protein. Nature 2016, 536, 104–107.
23. Liang, Y.L.; Khoshouei, M.; Radjainia, M.; Zhang, Y.; Glukhova, A.; Tarrasch, J.; Thal, D.M.; Furness, S.G.B.; Christopoulos, G.; Coudrat, T.; et al. Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature 2017, 546, 118–123.
24. Zhang, Y.; Sun, B.; Feng, D.; Hu, H.; Chu, M.; Qu, Q.; Tarrasch, J.T.; Li, S.; Kobilka, T.S.; Kobilka, B.K.; et al. Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein. Nature 2017, 546, 248–253.
25. Mahoney, J.P.; Sunahara, R.K. Mechanistic insights into GPCR-G protein interactions. Curr. Opin. Struct. Biol. 2016, 41, 247–254.
26. Chung, K.Y.; Rasmussen, S.G.; Liu, T.; Li, S.; DeVree, B.T.; Chae, P.S.; Calinski, D.; Kobilka, B.K.; Woods, V.L.J.; Sunahara, R.K. Conformational changes in the G protein Gs induced by the β2 adrenergic receptor. Nature 2011, 477, 611–615.
27. Westfield, G.H.; Rasmussen, S.G.; Su, M.; Dutta, S.; DeVree, B.T.; Chung, K.Y.; Calinski, D.; Velez-Ruiz, G.; Oleskie, A.N.; Pardon, E.; et al. Structural flexibility of the G alpha s alpha-helical domain in the β2-adrenoceptor Gs complex. Proc. Natl. Acad. Sci. USA 2011, 108, 16086–16091.
28. Van Eps, N.; Preininger, A.M.; Alexander, N.; Kaya, A.I.; Meier, S.; Meiler, J.; Hamm, H.E.; Hubbell, W.L. Interaction of a G protein with an activated receptor opens the interdomain interface in the α subunit. Proc. Natl. Acad. Sci. USA 2011, 108, 9420–9424.
29. Kaya, A.I.; Lokits, A.D.; Gilbert, J.A.; Iverson, T.M.; Meiler, J.; Hamm, H.E. A conserved phenylalanine as a relay between the α5 helix and the GDP binding region of heterotrimeric Gi protein α subunit. J. Biol. Chem. 2014, 289, 24475–24487.
30. Alexander, N.S.; Preininger, A.M.; Kaya, A.I.; Stein, R.A.; Hamm, H.E.; Meiler, J. Energetic analysis of the rhodopsin-G-protein complex links the α5 helix to GDP release. Nat. Struct. Mol. Biol. 2014, 21, 56–63.
31. Kaya, A.I.; Lokits, A.D.; Gilbert, J.A.; Iverson, T.M.; Meiler, J.; Hamm, H.E. A Conserved Hydrophobic Core in Gαi1 Regulates G Protein Activation and Release from Activated Receptor. J. Biol. Chem. 2016, 291, 19674–19686.
32. DeVree, B.T.; Mahoney, J.P.; Vélez-Ruiz, G.A.; Rasmussen, S.G.; Kuszak, A.J.; Edwald, E.; Fung, J.J.; Manglik, A.; Masureel, M.; Du, Y.; et al. Allosteric coupling from G protein to the agonist-binding pocket in GPCRs. Nature 2016, 535, 182–186.
33. Hamm, H.E.; Deretic, D.; Arendt, A.; Hargrave, P.A.; Koenig, B.; Hofmann, K.P. Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 1988, 241, 832–835.
34. Conklin, B.R.; Farfel, Z.; Lustig, K.D.; Julius, D.; Bourne, H.R. Substitution of three amino acids switches receptor specificity of Gqα to that of Giα. Nature 1993, 363, 274–276.
35. Liu, J.; Conklin, B.R.; Blin, N.; Yun, J.; Wess, J. Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation. Proc. Natl. Acad. Sci. USA 1995, 92, 11642–11646.
36. Coward, P.; Chan, S.D.; Wada, H.G.; Humphries, G.M.; Conklin, B.R. Chimeric G proteins allow a high-throughput signaling assay of Gi-coupled receptors. Anal. Biochem. 1999, 270, 242–248.
37. Scheerer, P.; Park, J.H.; Hildebrand, P.W.; Kim, Y.J.; Krauss, N.; Choe, H.W.; Hofmann, K.P.; Ernst, O.P. Crystal structure of opsin in its G-protein-interacting conformation. Nature 2008, 455, 497–502.
38. Choe, H.W.; Kim, Y.J.; Park, J.H.; Morizumi, T.; Pai, E.F.; Krauss, N.; Hofmann, K.P.; Scheerer, P.; Ernst, O.P. Crystal structure of metarhodopsin II. Nature 2011, 471, 651–655.
39. Hewavitharana, T.; Wedegaertner, P.B. Non-canonical signaling and localizations of heterotrimeric G proteins. Cell. Signal. 2012, 24, 25–34.
40. Gurevich, E.V.; Tesmer, J.J.; Mushegian, A.; Gurevich, V.V. G protein-coupled receptor kinases: More than just kinases and not only for GPCRs. Pharmacol. Ther. 2012, 133, 40–46.
41. 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 2015, 54, 4320–4329.
42. Kim, J.; Ahn, S.; Ren, X.R.; Whalen, E.J.; Reiter, E.; Wei, H.; Lefkowitz, R.J. Functional antagonism of different G protein-coupled receptor kinases for β-arrestin-mediated angiotensin II receptor signaling. Proc. Nat. Acad. Sci. USA 2005, 102, 1442–1447.
43. Ren, X.R.; Reiter, E.; Ahn, S.; Kim, J.; Chen, W.; Lefkowitz, R.J. Different G protein-coupled receptor kinases govern G protein and β-arrestin mediated signaling of V2 vasopressin receptor. Proc. Nat. Acad. Sci. USA 2005, 102, 1448–1453.
44. Sterne-Marr, R.; Leahey, P.A.; Bresee, J.E.; Dickson, H.M.; Ho, W.; Ragusa, M.J.; Donnelly, R.M.; Amie, S.M.; Krywy, J.A.; Brookins-Danz, E.D.; et al. GRK2 activation by receptors: Role of the kinase large lobe and carboxyl-terminal tail. Biochemistry 2009, 48, 4285–4293.
45. Palczewski, K.; Buczylko, J.; Kaplan, M.W.; Polans, A.S.; Crabb, J.W. Mechanism of rhodopsin kinase activation. J. Biol. Chem. 1991, 266, 12949–12955.
46. Boguth, C.A.; Singh, P.; Huang, C.C.; Tesmer, J.J. Molecular basis for activation of G protein-coupled receptor kinases. EMBO J. 2010, 29, 3249–3259.
47. He, Y.; Gao, X.; Goswami, D.; Hou, L.; Pal, K.; Yin, Y.; Zhao, G.; Ernst, O.P.; Griffin, P.; Melcher, K.; et al. Molecular assembly of rhodopsin with G protein-coupled receptor kinases. Cell Res. 2017, 27, 728–747.
48. Han, M.; Gurevich, V.V.; Vishnivetskiy, S.A.; Sigler, P.B.; Schubert, C. Crystal structure of β-arrestin at 1.9 A: Possible mechanism of receptor binding and membrane translocation. Structure 2001, 9, 869–880.
49. Hirsch, J.A.; Schubert, C.; Gurevich, V.V.; Sigler, P.B. The 2.8 Å crystal structure of visual arrestin: A model for arrestin’s regulation. Cell 1999, 97, 257–269.
50. Sutton, R.B.; Vishnivetskiy, S.A.; Robert, J.; Hanson, S.M.; Raman, D.; Knox, B.E.; Kono, M.; Navarro, J.; Gurevich, V.V. Crystal Structure of Cone Arrestin at 2.3 Å: Evolution of Receptor Specificity. J. Mol. Biol. 2005, 354, 1069–1080.
51. 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 arrestins. J. Mol. Biol. 2011, 406, 467–478.
52. Schleicher, A.; Kuhn, H.; Hofmann, K.P. Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II. Biochemistry 1989, 28, 1770–1775.
53. Palczewski, K.; Pulvermuller, A.; Buczylko, J.; Hofmann, K.P. Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin. J. Biol. Chem. 1991, 266, 18649–18654.
54. Gurevich, V.V.; Benovic, J.L. Visual arrestin interaction with rhodopsin: Sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin. J. Biol. Chem. 1993, 268, 11628–11638.
55. Modzelewska, A.; Filipek, S.; Palczewski, K.; Park, P.S. Arrestin interaction with rhodopsin: Conceptual models. Cell Biochem. Biophys. 2006, 46, 1–15.
56. Hanson, S.M.; Francis, D.J.; Vishnivetskiy, S.A.; Kolobova, E.A.; Hubbell, W.L.; Klug, C.S.; Gurevich, V.V. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc. Natl. Acad. Sci. USA 2006, 103, 4900–4905.
57. 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. 2014, 289, 20991–21002.
58. Zhuang, T.; Chen, Q.; Cho, M.-K.; Vishnivetskiy, S.A.; Iverson, T.I.; Gurevich, V.V.; Hubbell, W.L. Involvement of Distinct Arrestin-1 Elements in Binding to Different Functional Forms of Rhodopsin. Proc. Nat. Acad. Sci. USA 2013, 110, 942–947.
59. Gurevich, V.V.; Gurevich, E.V. The structural basis of arrestin-mediated regulation of G protein-coupled receptors. Pharmacol. Ther. 2006, 110, 465–502.
60. 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.; et al. Conformation of receptor-bound visual arrestin. Proc. Nat. Acad. Sci. USA 2012, 109, 18407–18412.
61. Shukla, A.K.; Manglik, A.; Kruse, A.C.; Xiao, K.; Reis, R.I.; Tseng, W.C.; Staus, D.P.; Hilger, D.; Uysal, S.; Huang, L.Y.; et al. Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 2013, 497, 137–141.
62. Vishnivetskiy, S.A.; Baameur, F.; Findley, K.R.; Gurevich, V.V. Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. J. Biol. Chem. 2013, 288, 11741–11750.
63. Granzin, J.; Cousin, A.; Weirauch, M.; Schlesinger, R.; Büldt, G.; Batra-Safferling, R. Crystal structure of p44, a constitutively active splice variant of visual arrestin. J. Mol. Biol. 2012, 416, 611–618.
64. Kim, Y.J.; Hofmann, K.P.; Ernst, O.P.; Scheerer, P.; Choe, H.W.; Sommer, M.E. Crystal structure of pre-activated arrestin p44. Nature 2013, 497, 142–146.
65. 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.; et al. Structural basis of arrestin-3 activation and signaling. Nat. Commun. 2017, 8, 1427.
66. Vishnivetskiy, S.A.; Hirsch, J.A.; Velez, M.-G.; Gurevich, Y.V.; Gurevich, V.V. Transition of arrestin in the active receptor-binding state requires an extended interdomain hinge. J. Biol. Chem. 2002, 277, 43961–43968.
67. Hanson, S.M.; Cleghorn, W.M.; Francis, D.J.; Vishnivetskiy, S.A.; Raman, D.; Song, X.; Nair, K.S.; Slepak, V.Z.; Klug, C.S.; Gurevich, V.V. Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. J. Mol. Biol. 2007, in press.
68. Shukla, A.K.; Westfield, G.H.; Xiao, K.; Reis, R.I.; Huang, L.Y.; Tripathi-Shukla, P.; Qian, J.; Li, S.; Blanc, A.; Oleskie, A.N.; et al. Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature 2014, 512, 218–222.
69. Szczepek, M.; Beyriere, F.; Hofmann, K.P.; Elgeti, M.; Kazmin, R.; Rose, A.; Bartl, F.J.; von Stetten, D.; Heck, M.; Sommer, M.E.; et al. Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nat. Commun. 2014, 5, 4801.
70. Lally, C.C.; Bauer, B.; Selent, J.; Sommer, M.E. C-edge loops of arrestin function as a membrane anchor. Nat. Commun. 2017, 8, 14258.
71. 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.; et al. Structural Identification of Phosphorylation Codes for Arrestin Recruitment by G protein-Coupled Receptors. Cell 2017, in press.
72. 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. 2007, 282, 32075–32083.
73. Mendez, A.; Burns, M.E.; Roca, A.; Lem, J.; Wu, L.W.; Simon, M.I.; Baylor, D.A.; Chen, J. Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites. Neuron 2000, 28, 153–164.
74. Gurevich, V.V.; Benovic, J.L. Visual arrestin binding to rhodopsin: Diverse functional roles of positively charged residues within the phosphorylation-recignition region of arrestin. J. Biol. Chem. 1995, 270, 6010–6016.
75. Gurevich, V.V.; Benovic, J.L. Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state. Mol. Pharmacol. 1997, 51, 161–169.
76. 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. 2000, 275, 41049–41057.
77. 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. 2011, 286, 24288–24299.
78. 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. 1997, 272, 23682–23689.
79. Lee, K.B.; Ptasienski, J.A.; Pals-Rylaarsdam, R.; Gurevich, V.V.; Hosey, M.M. Arrestin binding to the M2 muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor. J. Biol. Chem. 2000, 275, 9284–9289.
80. Gurevich, V.V.; Gurevich, E.V. Arrestins: Discovery of The Family and Functional Role of Conformational flexibility. In The Structural Basis of Arrestin Functions; Gurevich, V.V., Ed.; Springer: Berlin/Heidelberg, Germany, 2017; pp. 3–18. ISBN 978-3-319-57552-0.
81. Gurevich, E.V.; Gurevich, V.V. Arrestins are ubiquitous regulators of cellular signaling pathways. Genome Biol. 2006, 7, 236.
82. Milano, S.K.; Pace, H.C.; Kim, Y.M.; Brenner, C.; Benovic, J.L. Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 2002, 41, 3321–3328.
83. Peterhans, C.; Lally, C.C.; Ostermaier, M.K.; Sommer, M.E.; Standfuss, J. Functional map of arrestin binding to phosphorylated opsin, with and without agonist. Sci. Rep. 2016, 6, 2868.
84. Vishnivetskiy, S.A.; Hosey, M.M.; Benovic, J.L.; Gurevich, V.V. Mapping the arrestin-receptor interface: Structural elements responsible for receptor specificity of arrestin proteins. J. Biol. Chem. 2004, 279, 1262–1268.
85. Schoneberg, T.; Schulz, A.; Biebermann, H.; Hermsdorf, T.; Rompler, H.; Sangkuhl, K. Mutant G-protein-coupled receptors as a cause of human diseases. Pharmacol. Ther. 2004, 104, 173–206.
86. Stoy, H.; Gurevich, V.V. How genetic errors in GPCRs affect their function: Possible therapeutic strategies. Genes Dis. 2015, 2, 108–132.
87. 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. 2009, 19, 700–705.
88. Gimenez, L.E.; Vishnivetskiy, S.A.; Baameur, F.; Gurevich, V.V. Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins. J. Biol. Chem. 2012, 287, 29495–29505.
89. 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. 2014, 26, 1523–1531.
90. 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. 2017, 36, 98–107.
91. DeWire, S.M.; Ahn, S.; Lefkowitz, R.J.; Shenoy, S.K. β-arrestins and cell signaling. Annu. Rev. Physiol. 2007, 69, 483–510.
92. Peterson, Y.K.; Luttrell, L.M. The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling. Pharmacol. Rev. 2017, 69, 256–297.
93. McDonald, P.H.; Chow, C.W.; Miller, W.E.; Laporte, S.A.; Field, M.E.; Lin, F.T.; Davis, R.J.; Lefkowitz, R.J. β-arrestin 2: A receptor-regulated MAPK scaffold for the activation of JNK3. Science 2000, 290, 1574–1577.
94. Song, X.; Coffa, S.; Fu, H.; Gurevich, V.V. How does arrestin assemble MAPKs into a signaling complex? J. Biol. Chem. 2009, 284, 685–695.
95. Seo, J.; Tsakem, E.L.; Breitman, M.; Gurevich, V.V. Identification of arrestin-3-specific residues necessary for JNK3 kinase activation. J. Biol. Chem. 2011, 286, 27894–27901.
96. 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. 2012, 287, 19653–19664.
97. 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. 2014, 21, 172–184.
98. Danial, N.N.; Korsmeyer, S.J. Cell death: Critical control points. Cell 2004, 116, 205–219.
99. Zhan, X.; Perez, A.; Gimenez, L.E.; Vishnivetskiy, S.A.; Gurevich, V.V. Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains. Cell. Signal. 2014, 26, 766–776.
100. 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.; et al. Peptide mini-scaffold facilitates JNK3 activation in cells. Sci. Rep. 2016, 6, 21025.
101. 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 2015, 26, 622–635.