Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β- TrCP

Genes and Development

Volumn 13, Issue 3, 1999, Pages 284-294

  Spencer, Erika ^a   Jiang, Jin ^a   Chen, Zhijian J ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

I B; NF B; Phosphorylation; SCF; Slimb; Ubiquitin; TrCP

Indexed keywords

BETA TRCP; CALYCULIN A; CELL CYCLE PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SLIMB PROTEIN; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DROSOPHILA; EMBRYO; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; TRANSCRIPTION REGULATION;

ANIMALIA; GASTROPODA; VERTEBRATA;

EID: 0033083158     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.13.3.284     Document Type: Article

References (50)

1. Aberle, H., A. Bauer, J. Stappert, A. Kispert, and R. Kemler. 1997. β-Catenin is a target for the Ub-proteasome pathway. EMBO J. 16: 3797-3804.
2. Alkalay, I., A. Yaron, A. Hatzubai, A. Orian, A. Ciechanover, and Y. Ben-Neriah. 1995. Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the Ub-proteasome pathway. Proc. Natl. Acad. Sci. 92: 10599-10603.
3. Aza-Blanc, P., F.A. Ramirez-Weber, M.P. Laget, C. Schwartz, and T.B. Kornberg. 1997. Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor. Cell 89: 1043-1053.
4. Baeuerle, P. and D. Baltimore. 1996. NF-κB: Ten years after. Cell 87: 13-20.
5. Bai, C., P. Sen, K. Hofmann, L. Ma, M. Goebl, J.W. Harper, and S.J. Elledge. 1996. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86: 263-274.
6. Baldwin, A.S. 1996. The NF-κB and IκB proteins: New discoveries and insights. Annu. Rev. Immunol. 14: 649-681.
7. Brockman, J.A., D.C. Scherer, T.A. McKinsey, S.M. Hall, X. Qi, W.Y. Lee, and D.W. Ballard. 1995. Coupling of a signal response domain in IκBα to multiple pathways for NF-κB activation. Mol. Cell. Biol. 15: 2809-2818.
8. Chau, V., J.W. Tobias, A. Bachmair, D. Marriott, D.J. Ecker, D.K. Gonda, and A. Varshavsky. 1989. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576-1583.
9. Chen, Z.J., J. Hagler, V.J. Palombella, F. Melandri, D. Scherer, D. Ballard, and T. Maniatis. 1995. Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway. Genes & Dev. 9: 1586-1597.
10. Chen, Z.J., L. Parent, and T. Maniatis. 1996 Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell 84: 853-862.
11. Chou, T.-B. and N. Perrimon. 1992. Use of a yeast site-specific recombinase to produce female germline chimeras in Drosophila. Genetics 131: 643-653.
12. Ciechanover, A., Y. Hod, and A. Hershko. 1978. A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem. Biophys. Res. Commun. 81: 1100-1105.
13. Feldman, R.M., C.C. Correll, K.B. Kaplan, and R.J. Deshaies. 1997. A complex of Cdc4p, Skp1p, and Cdc53p/Cullin catalyzes Ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 9: 221-230.
14. Haskill, S., A.A. Beg, S.N. Tompkins, J.S. Morris, A.D. Yurochko, A. Sampson-Johannes, K. Mondai, P. Ralph, and A.S. Baldwin. 1991. Characterization of an immediate-early gene induced in adherent monocytes that encodes IκB-like activities. Cell 65: 1281-1289.
15. Hershko, A. and A. Ciechanover. 1998. The ubiquitin system. Annu. Rev. Biochem. 67: 425-479.
16. Hershko, A., A. Ciechanover, H. Heller, A.L. Haas, and I.A. Rose. 1980. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc. Natl. Acad. Sci. 77: 1783-1786.
17. Hershko, A., D. Ganoth, V. Sudakin, A. Dahan, L.H. Cohen, F.C. Luca, J.V. Ruderman, and E. Eytan. 1994. Components of a system that ligates cyclin to ubiquitin and their regulation by the protein kinase cdc2. J. Biol. Chem. 269: 4940-4946.
18. Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30: 405-439.
19. Jackson, P.K. 1996. Cell cycle: cull and destroy. Curr. Biol. 6: 1209-1212.
20. Jiang, J. and G. Struhl. 1998. Regulation of the Hedgehog and Wingless signaling pathways by the F-box/WD40-repeat protein Slimb. Nature 391: 493-496.
21. Jiang, J., D. Kosman, Y.T. Ip, and M. Levine. 1991. The dorsal morphogen gradient regulates the mesoderm determinant twist in early Drosophila embryos. Genes & Dev. 5: 1881-1891.
22. Kipreos, E.T., L.E. Lander, J.P. Wing, W.W. He, and E.M. Hedgecock. 1996. cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. Cell 85: 829-839.
23. King, R.W., J.M. Peters, S. Tugendreich, M. Rolfe, P. Hieter, and M.W. Kirschner. 1995. A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B. Cell 81: 279-288.
24. Lam, Y.A., G.N. DeMartino, C.M. Pickart, and R.E. Cohen. 1997. Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26 S proteasomes. J. Biol. Chem. 272: 28438-28446.
25. Lee, F.S., J. Hagler, Z. Chen, and T. Maniatis. 1997. Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell 88: 213-222.
26. Maniatis, T. 1997. Catalysis by a multiprotein IκB kinase complex. Science 278: 818-819.
27. Margottin, F., S.P. Bour, H. Durand, L. Selig, S. Benichou, V. Richard, D. Thomas, K. Strebel, and R. Benarous. 1998. A novel human WD protein, h-βTRCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-Box motif. Mol. Cell 1: 565-574.
28. Morisato, D. and K.V. Anderson. 1995. Signaling pathways that establish the dorsal-ventral pattern of the Drosophila embryo. Annu. Rev. Genet. 29: 371-379.
29. Nusse, R. 1997. A versatile transcriptional effector of Wingless signaling. Cell 89: 321-323.
30. Orford, K., C. Crockett, J.P. Jensen, A.M. Weissman, and S.W. Byers. 1997. Serine phosphorylation-regulated ubiquitination and degradation of β-catenin. J. Biol. Chem. 272: 24735-24738.
31. Palombella, V.J., O.J. Rando, A.L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78: 773-785.
32. Patton, E., A.R. Willems, and M. Tyers. 1998. Combinatorial control in ubiquitin-dependent proteolysis: Don't Skp the F-box hypothesis. Trends Genet. 14: 236-243.
33. Pickart, C.M. 1997. Targeting of substrates to the 26S proteasome. FASEB J. 11: 1055-1066.
34. Ray, R.P., K. Arora, C. Nüsslein-Volhard, and W.M. Gelbart. 1991. The control of cell fate along the dorsal-ventral axis of the Drosophila embryo. Development 113: 35-54.
35. Roth, S., Y. Hiromi, D. Godt, and C. Nüsslein-Volhard. 1991. cactus, a maternal gene required for proper formation of the dorsoventral morphogen gradient in Drosophila embryos. Development 112: 371-388.
36. Sambrook, J., E.F. Fritsch, and T. Maniatis. 1989. Molecular cloning: A laboratory manual Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
37. Scheidereit, C. 1998. Signal transduction. Docking IκB kinases. Nature 395: 225-226.
38. Scherer, D.C., J.A. Brockman, Z.J. Chen, T. Maniatis, and D. Ballard. 1995. Signal-induced degradation of IκBα requires site-specific ubiquitination. Proc. Natl. Acad. Sci. 92: 11259-11263.
39. Scott, M.L., T. Fujita, H.C. Liou, G.P. Nolan, and D. Baltimore. 1993. The p65 subunit of NF-κB regulates IκB by two distinct mechanisms. Genes & Dev. 7: 1266-1276.
40. Skowyra, D., K.L. Craig, M. Tyers, S.J. Elledge, and J.W. Harper. 1997. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91: 209-219.
41. Spevak, W., B.D. Keiper, C. Stratowa, and M.J. Castanon. 1993. Saccharomyces cerevisiae cdc15 mutants arrested at a late stage in anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with β-transducin repeats. Mol. Cell. Biol. 13: 4953-4966.
42. Stancovski, I. and D. Baltimore. 1997. NF-κB activation: the IκB kinase revealed? Cell 91: 299-302.
43. Thanos, D. and T. Maniatis. 1992. The high mobility group protein HMG I(Y) is required for NF-κB dependent virus induction of the human IFN-β gene. Cell 71: 777-789.
44. Theodosiou, N.A., S. Zhang, W.Y. Wang, and T. Xu. 1998. slimb coordinates wg and dpp expression in the dorsal-ventral and anterior-posterior axes during limb development. Development 125: 3411-34166.
45. Traenckner, E.B., H.L. Pahl, T. Henkel, K.M. Schmidt, S. Wilk, and P.A. Baeuerle. 1995. Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14: 2876-2883.
46. Wang, D. and A.S. Baldwin, Jr. 1998. Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529. J. Biol. Chem. 273: 29411-29416.
47. Wilkinson, K.D., M.K. Urban, and A.L. Haas. 1980. Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. J Biol. Chem. 255: 7529-7532.
48. Yaron, A., H. Gonen, I. Alkalay, A. Hatzubai, S. Jung, S. Beyth, F. Mercurio, A.M. Manning, A. Ciechanover, and Y. BenNeriah. 1997. Inhibition of NF-κB cellular function via specific targeting of the IκB-ubiquitin ligase. EMBO J. 16: 6486-6494.
49. Zhong, H., H. SuYang, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1997. The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell 89: 413-424.
50. Zhou, P. and P. Howley. 1998. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell. 2: 571-580.