β-Arrestin-kinase scaffolds: Turn them on or turn them off?

Wiley Interdisciplinary Reviews: Systems Biology and Medicine

Volumn 5, Issue 2, 2013, Pages 231-241

  Lin, Alice ^a   Defea, Kathryn A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA ARRESTIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; COFILIN; G PROTEIN COUPLED RECEPTOR; LIM KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 10; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; RAF PROTEIN;

ARTICLE; CELL ACTIVITY; CELL PROLIFERATION; CELLULAR DISTRIBUTION; CONFORMATIONAL TRANSITION; ENZYME INHIBITION; ENZYME MECHANISM; NONHUMAN; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; REGULATORY MECHANISM;

ARRESTINS; PROTEIN-SERINE-THREONINE KINASES; SIGNAL TRANSDUCTION;

EID: 84873831497     PISSN: 19395094     EISSN: 1939005X     Source Type: Journal    
DOI: 10.1002/wsbm.1203     Document Type: Article

References (60)

1. Lefkowitz RJ, Shenoy SK. Transduction of receptor signals by β-arrestins. Science 2005, 308:512-517.
2. Shukla AK, Xiao K, Lefkowitz RJ. Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling. Trends Biochem Sci 2011, 36:457-469.
3. DeFea KA. β-Arrestins as regulators of signal termination and transduction: how do they determine what to scaffold? Cell Signal 2011, 23:621-629.
4. Defea K. β-Arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction. Br J Pharmacol 2008, 153(suppl 1):S298-S309.
5. Shenoy SK, Lefkowitz RJ. Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling. Biochem J 2003, 375(Pt 3):503-515.
6. Shenoy SK, Lefkowitz RJ. Seven-transmembrane receptor signaling through β-arrestin. Sci STKE 2005, 2005:cm10.
7. DeWire SM, Ahn S, Lefkowitz RJ, Shenoy S. β-Arrestins and cell signaling. Annu Rev Physiol 2007, 69:483-510.
8. Terai K, Matsuda M. Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase. EMBO Rep 2005, 6:251-255.
9. Winkler DG, Cutler RE, Drugan JK, Campbell S, Morrison DK, Cooper JA. Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity. J Biol Chem 1998, 273:21578-21584.
10. Luttrell LM, et al. β-Arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes. Science 1999, 283: 655-661.
11. Basu A, Sivaprasad U. Protein kinase Cε makes the life and death decision. Cell Signal 2007, 19: 1633-1642
12. Zang M, et al. Characterization of Ser338 phosphorylation for Raf-1 activation. J Biol Chem 2008, 283:31429-31437.
13. Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ. Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds. Proc Natl Acad Sci U S A 2001, 98:2449-2454.
14. Luttrell LM. 'Location, location, location': activation and targeting of MAP kinases by G protein-coupled receptors. J Mol Endocrinol 2003, 30:117-126.
15. DeFea KA, Zalevsky J, Thoma MS, Dery O, Mullins RD, Bunnett NW. β -Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J Cell Biol 2000, 148:1267-1281.
16. Tohgo A, Pierce KL, Choy EW, Lefkowitz RJ, Luttrell LM. β-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK-mediated transcription following angiotensin AT1a receptor stimulation. J Biol Chem 2002, 277:9429-9436.
17. Tohgo A, Choy EW, Gesty-Palmer D, Pierce KL, Laporte S, Oakley RH, Caron MG, Lefkowitz RJ, Luttrell LM. The stability of the G protein-coupled receptor-β-arrestin interaction determines the mechanism and functional consequence of ERK activation. J Biol Chem 2003, 278:6258-6267.
18. DeFea KA, Vaughn ZD, O'Bryan EM, Nishijima D, Dery O, Bunnett NW. The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β -arrestin-dependent scaffolding complex. Proc Natl Acad Sci U S A 2000, 97:11086-11091.
19. Ahn S, Maudsley S, Luttrell LM, Lefkowitz RJ, Daaka Y. Src-mediated tyrosine phosphorylation of dynamin is required for β2-adrenergic receptor internalization and mitogen-activated protein kinase signaling. J Biol Chem 1999, 274:1185-1188.
20. Gesty-Palmer D, et al. Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation. J Biol Chem 2006, 281:10856-10864.
21. Rajagopal S, Kim J, Ahn S, Craig S, Lam CM, Gerard NP, Gerard C, Lefkowitz RJ. β-Arrestin- but not G protein-mediated signaling by the "decoy" receptor CXCR7. Proc Natl Acad Sci U S A 2010, 107:628-632.
22. Bolger GB, et al. Scanning peptide array analyses identify overlapping binding sites for the signalling scaffold proteins, β-arrestin and RACK1, in cAMP-specific phosphodiesterase PDE4D5. Biochem J 2006, 398: 23-36.
23. Song X, Coffa S, Fu H, Gurevich VV. How does arrestin assemble MAPKs into a signaling complex? J Biol Chem 2009, 284:685-695.
24. Xu TR, Baillie GS, Bhari N, Houslay TM, Pitt AM, Adams DR, Kolch W, Houslay MD, Milligan G. Mutations of β-arrestin 2 that limit self-association also interfere with interactions with the β2-adrenoceptor and the ERK1/2 MAPKs: implications for β2-adrenoceptor signalling via the ERK1/2 MAPKs. Biochem J 2008, 413:51-60.
25. Li X, et al. A scanning peptide array approach uncovers association sites within the JNK/β arrestin signalling complex. FEBS Lett 2009, 583:3310-3316.
26. Meng D, Lynch MJ, Huston E, Beyermann M, Eichhorst J, Adams DR, Klussmann E, Houslay MD, Baillie GS. MEK1 binds directly to βarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization. J Biol Chem 2009, 284:11425-11435.
27. Terrillon S, Bouvier M. Receptor activity-independent recruitment of [β]arrestin2 reveals specific signalling modes. EMBO J 2004, 23:3950-3961.
28. 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 2011, 6:e28723.
29. Coffa S, Breitman M, Spiller BW, Gurevich VV. A single mutation in Arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding. Biochemistry 2011, 50:6951-6958.
30. Daaka Y, Luttrell LM, Ahn S, Della Rocca GJ, Ferguson SSG, Caron MG, Lefkowitz RJ. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J Biol Chem 1998, 273: 685-688.
31. McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ. β-Arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science 2000, 290:1574-1577.
32. Miller WE, McDonald PH, Cai SF, Field ME, Davis RJ, Lefkowitz RJ. Identification of a motif in the carboxyl terminus of β -arrestin2 responsible for activation of JNK3. J Biol Chem 2001, 276:27770-27777.
33. Seo J, Tsakem EL, Breitman M, Gurevich VV. Identification of arrestin-3-specific residues necessary for JNK3 kinase activation. J Biol Chem 2011, 286:27894-27901.
34. Willoughby EA, Collins MK. Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein β-arrestin 2. J Biol Chem 2005, 280:25651-25658.
35. Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. Crystal structure of β-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. Structure 2001, 9:869-880.
36. Gurevich VV, Gurevich EV. The molecular acrobatics of arrestin activation. Trends Pharmacol Sci 2004, 25:105-111.
37. 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 2011, 406: 467-478.
38. Shukla AK, Violin JD, Whalen EJ, Gesty-Palmer D, Shenoy SK, Lefkowitz RJ. Distinct conformational changes in β-arrestin report biased agonism at seven-transmembrane receptors. Proc Natl Acad Sci U S A 2008, 105: 9988-9993.
39. Dikic I, Wakatsuki S, Walters KJ. Ubiquitin-binding domains [mdash] from structures to functions. Nat Rev Mol Cell Biol 2009, 10:659-671.
40. Miller WE, Maudsley S, Ahn S, Khan KD, Luttrell LM, Lefkowitz RJ. β-Arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of β-arrestin1-dependent targeting of c-SRC in receptor endocytosis. J Biol Chem 2000, 275:11312-11319.
41. Barlic J, Andrews JD, Kelvin AA, Bosinger SE, DeVries ME, Xu L, Dobransky T, Feldman RD. Regulation of tyrosine kinase activation and granule release through β-arrestin by CXCRI. Nat Immunol 2000, 1:227-233.
42. Wilde A, et al. EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake. Cell 1999, 96: 677-687.
43. Mellor P, Furber LA, Nyarko JN, Anderson DH. Multiple roles for the p85α isoform in the regulation and function of PI3K signalling and receptor trafficking. Biochem J 2012, 441:23-37.
44. Wang P, DeFea KA. Protease-activated receptor-2 simultaneously directs β-arrestin-1-dependent inhibition and Gαq-dependent activation of phosphatidylinositol 3-kinase. Biochemistry 2006, 45:9374-9385.
45. Wang P, Kumar P, Wang C, Defea KA. Differential regulation of class IA phosphoinositide 3-kinase catalytic subunits p110 α and β by protease-activated receptor 2 and β-arrestins. Biochem J 2007, 408:221-230.
46. Naga Prasad SV, Laporte SA, Chamberlain D, Caron MG, Barak L, Rockman HA. Phosphoinositide 3-kinase regulates β2-adrenergic receptor endocytosis by AP-2 recruitment to the receptor/β-arrestin complex. J Cell Biol 2002, 158:563-575.
47. Cheung R, Malik M, Ravyn V, Tomkowicz B, Ptasznik A, Collman RG. An arrestin-dependent multi-kinase signaling complex mediates MIP-1β/CCL4 signaling and chemotaxis of primary human macrophages. J Leukoc Biol 2009, 86:833-845.
48. Naga Prasad SV, Perrino C, Rockman HA. Role of phosphoinositide 3-kinase in cardiac function and heart failure. Trends Cardiovasc Med 2003, 13: 206-212.
49. Povsic TJ, Kohout TA, Lefkowitz RJ. β-Arrestin1 mediates insulin-like growth factor 1 (IGF-1) activation of phosphatidylinositol 3-kinase (PI3K) and anti-apoptosis. J Biol Chem 2003, 278:51334-51339.
50. Del'guidice T, Lemasson M, Beaulieu JM. Role of β-arrestin 2 downstream of dopamine receptors in the Basal Ganglia. Front Neuroanat 2011, 5:58.
51. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S. 1999. Signaling from Rho to the Actin Cytoskeleton Through Protein Kinases ROCK and LIM-kinase. Science 285: 895-898.
52. Li R, Soosairajah J, Harari D, Citri A, Price J, Ng HL, Morton CJ, Parker MW, Yarden Y, Bernard O. Hsp90 increases LIM kinase activity by promoting its homo-dimerization. FASEB J 2006, 20:1218-1220.
53. 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 2006, 364:955-963.
54. Xiao K, et al. Functional specialization of β-arrestin interactions revealed by proteomic analysis. Proc Natl Acad Sci U S A 2007, 104:12011-12016.
55. Mangmool S, Shukla AK, Rockman HA. β-Arrestin- dependent activation of Ca2+/calmodulin kinase II after β1-adrenergic receptor stimulation. J Cell Biol 2010, 189:573-587.
56. Wang P, Jiang Y, Wang Y, Shyy JY, DeFea KA. β-Arrestin inhibits CAMKKβ-dependent AMPK activation downstream of protease-activated-receptor-2. BMC Biochem 2010, 11:36.
57. Levchenko A, Bruck J, Sternberg PW. Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc Natl Acad Sci U S A 2000, 97: 5818-5823.
58. Vishnivetskiy SA, Paz CL, Schubert C, Hirsch JA, Sigler PB, Gurevich VV. How does arrestin respond to the phosphorylated state of rhodopsin? J Biol Chem 1999, 274:11451-11454.
59. Xiao K, et al. Global phosphorylation analysis of β-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR). Proc Natl Acad Sci U S A 2010, 107:15299-15304.
60. Christensen GL, Kelstrup CD, Lyngsø C, Sarwar U, Bøgebo R, Sheikh SP, Gammeltoft S, Olsen JV, Hansen JL. Quantitative phosphoproteomics dissection of 7TM receptor signaling using full and biased agonists. Mol Cell Proteomics 2010, 9:1540-1553.