Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation

Molecular Biology of the Cell

Volumn 28, Issue 8, 2017, Pages 1003-1010

  Kumari, Punita ^a   Srivastava, Ashish ^a   Ghosh, Eshan ^a   Ranjan, Ravi ^a   Dogra, Shalini ^b   Yadav, Prem N ^b   Shukla, Arun K ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

^b CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN BINDING FRAGMENT 30; AVP; BETA ARRESTIN 1; CLATHRIN; G PROTEIN COUPLED RECEPTOR; GLUTATHIONE TRANSFERASE; HORMONE RECEPTOR STIMULATING AGENT; MITOGEN ACTIVATED PROTEIN KINASE 1; TOLVAPTAN; UNCLASSIFIED DRUG; VASOPRESSIN V2 RECEPTOR; ARRB1 PROTEIN, HUMAN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN BINDING; RETINA S ANTIGEN; VASOPRESSIN RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENDOCYTOSIS; ENZYME ACTIVATION; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; FLUORESCENCE SPECTROSCOPY; HUMAN; IN VITRO STUDY; INTERNALIZATION; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RECEPTOR DOWN REGULATION; STEREOSPECIFICITY; WILD TYPE; AMINO ACID SEQUENCE; HEK293 CELL LINE; METABOLISM; PHOSPHORYLATION; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ARRESTINS; BETA-ARRESTIN 1; CLATHRIN; ENDOCYTOSIS; ENZYME ACTIVATION; GTP-BINDING PROTEINS; HEK293 CELLS; HUMANS; MAP KINASE SIGNALING SYSTEM; MITOGEN-ACTIVATED PROTEIN KINASE 1; PHOSPHORYLATION; PROTEIN BINDING; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, VASOPRESSIN;

EID: 85017690766     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E16-12-0818     Document Type: Article

References (39)

1. Bjarnadottir TK, Gloriam DE, Hellstrand SH, Kristiansson H, Fredriksson R, Schioth HB (2006). Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse. Genomics 88, 263-273.
2. Bockaert J, Pin JP (1999). Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J 18, 1723-1729.
3. Butcher AJ, Kong KC, Prihandoko R, Tobin AB (2012). Physiological role of G-protein coupled receptor phosphorylation. Handb Exp Pharmacol 79-94.
4. Coffa S, Breitman M, Hanson SM, Callaway K, Kook S, Dalby KN, Gurevich VV (2011). The effect of arrestin conformation on the recruitment of c- Raf1, MEK1, and ERK1/2 activation. PLoS One 6, e28723.
5. DeWire SM, Ahn S, Lefkowitz RJ, Shenoy SK (2007). Beta-arrestins and cell signaling. Annu Rev Physiol 69, 483-510.
6. Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG (1996). Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770.
7. Goodman OB Jr, Krupnick JG, Santini F, Gurevich VV, Penn RB, Gagnon AW, Keen JH, Benovic JL (1996). Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature 383, 447-450.
8. Gurevich EV, Tesmer JJ, Mushegian A, Gurevich VV (2012). G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharmacol Ther 133, 40-69.
9. Gurevich VV, Gurevich EV (2004). The molecular acrobatics of arrestin activation. Trends Pharmacol Sci 25, 105-111.
10. Gurevich VV, Gurevich EV (2013). Structural determinants of arrestin functions. Prog Mol Biol Transl Sci 118, 57-92.
11. Gurevich VV, Gurevich EV (2014). Extensive shape shifting underlies functional versatility of arrestins. Curr Opin Cell Biol 27, 1-9.
12. Kang DS, Tian X, Benovic JL (2014). Role of beta-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking. Curr Opin Cell Biol 27, 63-71.
13. Kang Y, Gao X, Zhou XE, He Y, Melcher K, Xu HE (2016). A structural snapshot of the rhodopsin-arrestin complex. FEBS J 283, 816-821.
14. Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, Barty A, White TA, Yefanov O, Han GW, et al. (2015). Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561-567.
15. Kim YJ, Hofmann KP, Ernst OP, Scheerer P, Choe HW, Sommer ME (2013). Crystal structure of pre-activated arrestin p44. Nature 497, 142-146.
16. Kumari P, Srivastava A, Banerjee R, Ghosh E, Gupta P, Ranjan R, Chen X, Gupta B, Gupta C, Jaiman D, Shukla AK (2016). Functional competence of a partially engaged GPCR-beta-arrestin complex. Nat Commun 7, 13416.
17. Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS (1999). The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. Proc Natl Acad Sci USA 96, 3712-3717.
18. Lefkowitz RJ (2007). Seven transmembrane receptors: something old, something new. Acta Physiol (Oxf) 190, 9-19.
19. Lefkowitz RJ, Shenoy SK (2005). Transduction of receptor signals by betaarrestins. Science 308, 512-517.
20. Lin A, DeFea KA (2013). beta-Arrestin-kinase scaffolds: turn them on or turn them off? Wiley Interdiscip Rev Syst Biol Med 5, 231-241.
21. Luttrell LM, Ferguson SS, Daaka Y, Miller WE, Maudsley S, Della Rocca GJ, Lin F, Kawakatsu H, Owada K, Luttrell DK, et al. (1999). Beta-arrestindependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science 283, 655-661.
22. Luttrell LM, Lefkowitz RJ (2002). The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci 115, 455-465.
23. Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ (2001). Activation and targeting of extracellular signalregulated kinases by beta-arrestin scaffolds. Proc Natl Acad Sci USA 98, 2449-2454.
24. Manglik A, Kobilka B (2014). The role of protein dynamics in GPCR function: insights from the beta2AR and rhodopsin. Curr Opin Cell Biol 27, 136-143.
25. McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ (2000). Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science 290, 1574-1577.
26. Nobles KN, Guan Z, Xiao K, Oas TG, Lefkowitz RJ (2007). The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2. J Biol Chem 282, 21370-21381.
27. Puig J, Arendt A, Tomson FL, Abdulaeva G, Miller R, Hargrave PA, McDowell JH (1995). Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin. FEBS Lett 362, 185-188.
28. Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, et al. (2011). Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 477, 549-555.
29. Ren XR, Reiter E, Ahn S, Kim J, Chen W, Lefkowitz RJ (2005). Different G protein-coupled receptor kinases govern G protein and beta-arrestinmediated signaling of V2 vasopressin receptor. Proc Natl Acad Sci USA 102, 1448-1453.
30. Shenoy SK, Lefkowitz RJ (2011). Beta-arrestin-mediated receptor trafficking and signal transduction. Trends Pharmacol Sci 32, 521-533.
31. Shukla AK, Manglik A, Kruse AC, Xiao K, Reis RI, Tseng WC, Staus DP, Hilger D, Uysal S, Huang LY, et al. (2013). Structure of active beta-arrestin- 1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497, 137-141.
32. Shukla AK, Westfield GH, Xiao K, Reis RI, Huang LY, Tripathi-Shukla P, Qian J, Li S, Blanc A, Oleskie AN, et al. (2014). Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature 512, 218-222.
33. Sinha A, Jones Brunette AM, Fay JF, Schafer CT, Farrens DL (2014). Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: Evidence for structural plasticity and multiple docking modes in arrestinrhodopsin binding. Biochemistry 53, 3294-3307.
34. Sommer ME, Farrens DL, McDowell JH, Weber LA, Smith WC (2007). Dynamics of arrestin-rhodopsin interactions: Loop movement is involved in arrestin activation and receptor binding. J Biol Chem 282, 25560-25568.
35. Sommer ME, Smith WC, Farrens DL (2005). Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events. J Biol Chem 280, 6861-6871.
36. Srivastava A, Gupta B, Gupta C, Shukla AK (2015). Emerging functional divergence of beta-arrestin Isoforms in GPCR function. Trends Endocrinol Metab 26, 628-642.
37. Szczepek M, Beyriere F, Hofmann KP, Elgeti M, Kazmin R, Rose A, Bartl FJ, von Stetten D, Heck M, Sommer ME, et al. (2014). Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nat Commun 5, 4801.
38. van Koppen CJ, Jakobs KH (2004). Arrestin-independent internalization of G protein-coupled receptors. Mol Pharmacol 66, 365-367.
39. Xiao K, Shenoy SK, Nobles K, Lefkowitz RJ (2004). Activation-dependent conformational changes in -β-arrestin 2. J Biol Chem 279, 55744-55753.