Regulated ubiquitination of proteins in GPCR-initiated signaling pathways

Trends in Pharmacological Sciences

Volumn 25, Issue 1, 2004, Pages 35-41

  Wojcikiewicz, Richard J H ^a  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETA ARRESTIN; CHEMOKINE RECEPTOR; CHEMOKINE RECEPTOR CXCR4; DELTA OPIATE RECEPTOR; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; MU OPIATE RECEPTOR; PROTEIN; PROTEIN KINASE C ALPHA; PROTEIN KINASE C DELTA; PROTEIN KINASE C EPSILON; PROTEIN P53; PROTEIN SUBUNIT; PROTEINASE; PROTIRELIN RECEPTOR; RGS PROTEIN; RHODOPSIN; TRANSDUCIN; UBIQUITIN; VASOPRESSIN V2 RECEPTOR;

APOPTOSIS; CELL CYCLE; CELL FUNCTION; CELL VIABILITY; DRUG APPROVAL; ENDOCYTOSIS; ENDOPLASMIC RETICULUM; LYSOSOME; MODULATION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; UBIQUITINATION;

EID: 0346655115     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2003.11.008     Document Type: Review

References (60)

1. Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
2. Weissman A.M. Themes and variations on ubiquitinylation. Nat. Rev. Mol. Cell Biol. 2:2001;169-178.
3. Di Fiore P., et al. When ubiquitin meets ubiquitin receptors: a signalling connection. Nat. Rev. Mol. Cell Biol. 4:2003;491-497.
4. Raiborg C., et al. Protein sorting into multivesicular endosomes. Curr. Opin. Cell Biol. 15:2003;446-455.
5. Fang S., et al. RING finger ubiquitin protein ligases: implications for tumorigenesis, metastasis and for molecular targets in cancer. Semin. Cancer Biol. 13:2003;5-14.
6. Jarosch E., et al. Endoplasmic reticulum-associated protein degradation. Int. Rev. Cytol. 223:2003;39-81.
7. Schubert U., et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature. 404:2000;770-774.
8. Mitchell B.S. The proteasome - an emerging therapeutic target in cancer. New Engl. J. Med. 348:2003;2597-2598.
9. 2-adrenergic receptor and β-arrestin. Science. 294:2001;1307-1313.
10. Marchese A., Benovic J.L. Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. J. Biol. Chem. 276:2001;45509-45512.
11. Martin N.P., et al. Regulation of V2 vasopressin receptor degradation by agonist promoted ubiquitination. J. Biol. Chem. 278:2003;45954-45959.
12. Shenoy S.K., Lefkowitz R.J. Trafficking patterns of β-arrestin and G protein-coupled receptors determined by the kinetics of β-arrestin deubiquitination. J. Biol. Chem. 278:2003;14498-14506.
13. Penela P., et al. Degradation of the G protein-coupled receptor kinase 2 by the proteasome pathway. J. Biol. Chem. 273:1998;35238-35244.
14. Bokkala S., Joseph S.K. Angiotensin II-induced down-regulation of inositol trisphosphate receptors in WB rat liver epithelial cells. J. Biol. Chem. 272:1997;12454-12461.
15. Oberdorf J.A., et al. Down-regulation of types I, II and III inositol 1,4,5 trisphosphate receptors is mediated by the ubiquitin / proteasome pathway. Biochem. J. 339:1999;453-461.
16. Wojcikiewicz R.J.H., et al. Ubiquitination and proteasomal degradation of endogenous and exogenous inositol 1,4,5-trisphosphate receptors in αT3-1 anterior pituitary cells. J. Biol. Chem. 278:2003;940-947.
17. 2+. J. Biol. Chem. 278:2003;38238-38246.
18. Lu Z., et al. Activation of protein kinase C triggers its ubiquitination and degradation. Mol. Cell. Biol. 18:1998;839-845.
19. Petaja-Repo U.E., et al. Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome. J. Biol. Chem. 276:2001;4416-4423.
20. Chaturvedi K., et al. Proteasome involvement in agonist-induced down-regulation of μ and δ opioid receptors. J. Biol. Chem. 276:2001;12345-12355.
21. Cook L.B., et al. Thyrotropin-releasing hormone receptor processing: role of ubiquitination and proteasomal degradation. Mol. Endocrinol. 17:2003;1777-1791.
22. Saliba R.S., et al. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J. Cell Sci. 115:2002;2907-2918.
23. Illing M.E., et al. A rhodopsin mutant linked to autosomal retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J. Biol. Chem. 277:2002;34150-34160.
24. Obin M., et al. Ubiquitinylation of the transducin βγ subunit complex. J. Biol. Chem. 277:2002;44566-44575.
25. Kim E., et al. Interaction between RGS7 and polycystin. Proc. Natl. Acad. Sci. U. S. A. 96:1999;6371-6376.
26. 2 subunit of G protein heterotrimer is an N-end rule ubiquitinylation substrate. Proc. Natl. Acad. Sci. U. S. A. 100:2003;5081-5086.
27. Li J.G., et al. Mechanisms of agonist-induced down-regulation of the human kappa opioid receptor: internalization is required for down-regulation. Mol. Pharmacol. 58:2000;795-801.
28. o subunits via the proteasome pathway is induced by the hsp90-specific compound geldanamycin. J. Biol. Chem. 275:2000;1565-1569.
29. i3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP. Proc. Natl. Acad. Sci. U. S. A. 100:2003;8270-8275.
30. Haglund K., et al. Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 5:2003;461-466.
31. Mosesson Y., et al. Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J. Biol. Chem. 278:2003;21323-21326.
32. Marotti L.A. Jr, et al. Direct identification of a G protein ubiquitination site by mass spectrometry. Biochemistry. 41:2002;5067-5074.
33. Roth A.F., Davis N.G. Ubiquitination of the yeast a-factor receptor. J. Cell Biol. 134:1996;661-674.
34. Hicke L., Riezman H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell. 84:1996;277-287.
35. Shenoy S.K., Lefkowitz R.J. Multifaceted roles of beta-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling. Biochem. J. 375:2003;503-515.
36. Raiborg C., et al. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nat. Cell Biol. 4:2002;394-398.
37. Wang P., et al. β-Arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2. J. Biol. Chem. 278:2003;6363-6370.
38. Van Kerkhof P., et al. Endocytosis and degradation of the growth hormone receptor are proteasome-dependent. J. Biol. Chem. 275:2000;1575-1580.
39. Van Kerkhof P., et al. Growth hormone receptor ubiquitination coincides with recruitment to clathrin-coated membrane domains. J. Biol. Chem. 276:2001;3778-3784.
40. Soubeyran P., et al. Cbl-CIN85-endophilin complex mediates ligand-induced down-regulation of EGF receptors. Nature. 416:2002;183-187.
41. Tanowitz M., von Zastrow M. Ubiquitination-independent trafficking of G protein-coupled receptors to lysosomes. J. Biol. Chem. 277:2002;50219-50222.
42. Tobin A.B. Are we β-ARKing up the wrong tree? Casein kinase 1 alpha provides an additional pathway for GPCR phosphorylation. Trends Pharmacol. Sci. 23:2002;337-343.
43. Hirsch C., Ploegh H.L. Intracellular targeting of the proteasome. Trends Cell Biol. 10:2000;268-272.
44. Tiwari S., Weissman A.M. Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. J. Biol. Chem. 276:2001;16193-16200.
45. Fang S., et al. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 98:2001;14422-14427.
46. Bays N.W., Hampton R.Y. Cdc48-Ufd1-Npl4: stuck in the middle with Ub. Curr. Biol. 12:2002;R366-R371.
47. Ye Y., et al. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162:2003;71-84.
48. Patel S., et al. Molecular properties of the inositol 1,4, 5-trisphosphate receptor. Cell Calcium. 25:1999;247-264.
49. Berridge M.J., et al. Calcium signalling: dynamics, homeostasis and remodeling. Nat. Rev. Mol. Cell Biol. 4:2003;517-529.
50. Wojcikiewicz R.J.H., et al. Muscarinic receptor activation down-regulates the type I inositol 1,4,5-trisphosphate receptor by accelerating its degradation. J. Biol. Chem. 269:1994;7963-7969.
51. Wojcikiewicz R.J.H. Type I, II and III inositol 1,4,5-trisphosphate receptors are unequally susceptible to down-regulation and are expressed in markedly different proportions in different cell types. J. Biol. Chem. 270:1995;11678-11683.
52. Sipma H., et al. Agonist-induced down-regulation of type 1 and type 3 inositol 1,4,5-trisphosphate receptors in A7r5 and DDT1 MF-2 smooth muscle cells. Cell Calcium. 23:1998;11-21.
53. Jellerette T., et al. Down-regulation of the inositol 1,4, 5-trisphosphate receptor in mouse eggs following fertilization or parthenogenetic activation. Dev. Biol. 223:2000;238-250.
54. Lee B., et al. Proteasomal activation mediates down-regulation of inositol 1,4,5-trisphosphate receptor and calcium mobilization in rat pancreatic islets. Endocrinology. 142:2001;1744-1751.
55. 3-activated elementary calcium signals and are downregulated by prolonged hormonal stimulation to inhibit cellular calcium responses. J. Cell Sci. 114:2001;3979-3989.
56. Wojcikiewicz R.J.H., et al. Secretagogues cause the ubiquitination and down-regulation of inositol 1,4,5 trisphosphate receptors in rat pancreatic acinar cells. Gastroenterology. 116:1999;1194-1201.
57. Shibao K., et al. Loss of inositol 1,4,5-trisphosphate receptors from bile duct epithelia is a common event in cholestasis. Gastroenterology. 125:2003;1175-1187.
58. Kaneko M., et al. Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. FEBS Lett. 532:2002;147-152.
59. Zhu C.C., et al. Inositol 1,4,5 trisphosphate receptor down-regulation is activated by binding of inositol 1,4,5 trisphosphate: studies with binding-defective receptor mutants. J. Biol. Chem. 274:1999;3476-3484.
60. Zhu C.C., Wojcikiewicz R.J.H. Ligand binding directly stimulates ubiquitination of the inositol 1,4,5 trisphosphate receptor. Biochem. J. 348:2000;551-556.