Structural Basis of Arrestin-Dependent Signal Transduction

Overview

Journal Trends Biochem Sci

Specialty Biochemistry

Date 2018 Apr 12

PMID 29636212

Citations 40

Authors

Qiuyan Chen

Tina M Iverson

Vsevolod V Gurevich

Affiliations

Soon will be listed here.

Abstract

Arrestins are a small family of proteins with four isoforms in humans. Remarkably, two arrestins regulate signaling from >800 G protein-coupled receptors (GPCRs) or nonreceptor activators by simultaneously binding an activator and one out of hundreds of other signaling proteins. When arrestins are bound to GPCRs or other activators, the affinity for these signaling partners changes. Thus, it is proposed that an activator alters arrestin's ability to transduce a signal. The comparison of all available arrestin structures identifies several common conformational rearrangements associated with activation. In particular, it identifies elements that are directly involved in binding to GPCRs or other activators, elements that likely engage distinct downstream effectors, and elements that likely link the activator-binding sites with the effector-binding sites.

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References

Indrischek H, Prohaska S, Gurevich V, Gurevich E, Stadler P . Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes. BMC Evol Biol. 2017; 17(1):163. PMC: 5501109. DOI: 10.1186/s12862-017-1001-4. View

Peterson Y, Luttrell L . The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling. Pharmacol Rev. 2017; 69(3):256-297. PMC: 5482185. DOI: 10.1124/pr.116.013367. View

Attramadal H, Arriza J, Aoki C, Dawson T, CODINA J, Kwatra M . Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family. J Biol Chem. 1992; 267(25):17882-90. View

Rasmussen S, DeVree B, Zou Y, Kruse A, Chung K, Kobilka T . Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature. 2011; 477(7366):549-55. PMC: 3184188. DOI: 10.1038/nature10361. View

Gurevich V . The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms. J Biol Chem. 1998; 273(25):15501-6. DOI: 10.1074/jbc.273.25.15501. View

Vishnivetskiy S, Raman D, Wei J, Kennedy M, Hurley J, Gurevich V . Regulation of arrestin binding by rhodopsin phosphorylation level. J Biol Chem. 2007; 282(44):32075-83. PMC: 2638115. DOI: 10.1074/jbc.M706057200. View

Nobles K, Xiao K, Ahn S, Shukla A, Lam C, Rajagopal S . Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. Sci Signal. 2011; 4(185):ra51. PMC: 3415961. DOI: 10.1126/scisignal.2001707. View

Luttrell L, Ferguson S, Daaka Y, Miller W, Maudsley S, Della Rocca G . Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science. 1999; 283(5402):655-61. DOI: 10.1126/science.283.5402.655. View

KOVOOR A, Celver J, Abdryashitov R, Chavkin C, Gurevich V . Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells. J Biol Chem. 1999; 274(11):6831-4. DOI: 10.1074/jbc.274.11.6831. View

10.

Kim Y, Hofmann K, Ernst O, Scheerer P, Choe H, Sommer M . Crystal structure of pre-activated arrestin p44. Nature. 2013; 497(7447):142-6. DOI: 10.1038/nature12133. View

11.

Gimenez L, Kook S, Vishnivetskiy S, Ahmed M, Gurevich E, Gurevich V . Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors. J Biol Chem. 2012; 287(12):9028-40. PMC: 3308753. DOI: 10.1074/jbc.M111.311803. View

12.

Ostermaier M, Peterhans C, Jaussi R, Deupi X, Standfuss J . Functional map of arrestin-1 at single amino acid resolution. Proc Natl Acad Sci U S A. 2014; 111(5):1825-30. PMC: 3918777. DOI: 10.1073/pnas.1319402111. View

13.

Hanson S, Gurevich V . The differential engagement of arrestin surface charges by the various functional forms of the receptor. J Biol Chem. 2005; 281(6):3458-62. PMC: 2440687. DOI: 10.1074/jbc.M512148200. View

14.

Sutton R, Vishnivetskiy S, Robert J, Hanson S, Raman D, Knox B . Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J Mol Biol. 2005; 354(5):1069-80. DOI: 10.1016/j.jmb.2005.10.023. View

15.

Tobin A, Butcher A, Kong K . Location, location, location...site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling. Trends Pharmacol Sci. 2008; 29(8):413-20. PMC: 2880250. DOI: 10.1016/j.tips.2008.05.006. View

16.

Xiao K, McClatchy D, Shukla A, Zhao Y, Chen M, Shenoy S . Functional specialization of beta-arrestin interactions revealed by proteomic analysis. Proc Natl Acad Sci U S A. 2007; 104(29):12011-6. PMC: 1913545. DOI: 10.1073/pnas.0704849104. View

17.

Laporte S, Oakley R, Zhang J, Holt J, Ferguson S, Caron M . The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. Proc Natl Acad Sci U S A. 1999; 96(7):3712-7. PMC: 22359. DOI: 10.1073/pnas.96.7.3712. View

18.

Goodman Jr O, Krupnick J, Santini F, Gurevich V, Penn R, Gagnon A . Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature. 1996; 383(6599):447-50. DOI: 10.1038/383447a0. View

19.

Liang Y, Khoshouei M, Radjainia M, Zhang Y, Glukhova A, Tarrasch J . Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature. 2017; 546(7656):118-123. PMC: 5832441. DOI: 10.1038/nature22327. View

20.

Zhuang T, Chen Q, Cho M, Vishnivetskiy S, Iverson T, Gurevich V . Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci U S A. 2013; 110(3):942-7. PMC: 3549108. DOI: 10.1073/pnas.1215176110. View