Control of NF-κB activity by the IkBβ inhibitor

Immunobiology

Volumn 198, Issue 1-3, 1997, Pages 14-23

  Weil, Robert ^a   Whiteside, Simon T ^a   Israël, Alain ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; HYBRIDOMA; MAMMAL CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; T LYMPHOCYTE;

EID: 0031435749     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0171-2985(97)80023-X     Document Type: Article

References (39)

1. WHITESIDE, S. T., J.-C. EPINAT, N. R. RICE, and A. ISRAËL. 1997. I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity. EMBO J. 16: 1413.
2. DECKHUT, A. M., W. ALLAN, A. MCMICKLE, M. EICHELBERGER, M. A. BLACKMAN, P. C. DOHERTY, and D. L. WOODLAND. 1993. Prominent usage of V beta 8.3 T cells in the H-2Db-restricted response to an influenza A virus nucleoprotein epitope. J. Immunol. 151: 2658.
3. WHITESIDE, S. T., M. K. ERNST, O. LEBAIL, C. LAURENT-WINTER, N. R. RICE, and A. ISRAËL. 1995. N- and C-Terminal Sequences Control Degradation of MAD3/I kappa B alpha in Response to Inducers of NF-kappa B Activity. Mol. and Cell. Biol. 15: 5339.
4. BALDWIN, A. S. J. 1996. The NF kappa B and kappa B proteins: new discoveries and insights. Annu. Rev. Immunol. 14: 649.
5. ISRAËL, A. 1995. A role for phosphorylation and degradation in the control of NF-kappa B activity. Trends Gen. 11: 203.
6. CAPOBIANCO, A. J., D. CHANG, G. MOSIALOS, and T. D. GILMORE. 1992. p105, the NF-kappa B p50 precursor protein, is one of the cellular proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells. J. Virol. 66: 3758.
7. RICE, N. R., M. L. MACKICHAN, and A. ISRAËL. 1992. The Precursor of NF-kappa B p50 has I kappa B-like functions. Cell 71: 243.
8. MERCURIO, F., J. A. DIDONATO, C. ROSETTE, and M. KARIN. 1993. p105 and p98 Precursor Protiens Play an Active Role in NF-kappa B Mediated Signal Transduction. Genes Dev. 7: 705.
9. SCHEINMAN, R. I., A. A. BEG, and A. S. BALDWIN. 1993. NF-kappa B p100 (Lyt-10) is a component of H2TF1 and can function as an I kappa B-like molecule. Mol. Cell. Biol. 13: 6089.
10. SIF, S., and T. D. GILMORE. 1993. NF-kappa B p100 is one of the high-molecular-weight proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells. J. Virol. 67: 7612.
11. DOBRZANSKI, P., R. P. RYSECK, and R. BRAVO. 1995. Specific inhibition of RelB/p52 transcriptional activity by the C-terminal domain of p100. Oncogene 10: 1003.
12. INOUE, J., L. D. KERR, A. KAKIZUKA, and I. M. VERMA. 1992. I kappa B gamma, a 70 kd protein identical to the C-terminal half of p110 NF-kappa B: a new member of the I kappa B family. Cell 68: 1109.
13. THOMPSON, J. E., R. J. PHILLIPS, H. ERDJUMENTBROMAGE, P. TEMPST, and S. GHOSH. 1995. I kappa B beta regulates the persistent response in a biphasic activation of NF-kappa B. Cell 80: 573.
14. MOLITOR, J. A., W. H. WALKER, S. DOERRE, D. W,. BALLARD, and W. C. GREENE. 1990. NF-kappa B: a family of inducible and differentially expressed enhancer-binding proteins in human T cells. Proc. Natl. Acad. Sci. USA 87: 10028.
15. ALKALAY, I., A. YARON, A. HATZUBAI, S. JUNG, A. AVRAHAM, O. GERLITZ, L. I. PASHUT, and N. Y. BENNERIAH. 1995. In vivo stimulation of I kappa B phosphorylation is not sufficient to activate NF-kappa B. Mol. Cell. Biol. 15: 1294.
16. DIDONATO, J. A., F. MERCURIO, and M. KARIN. 1995. Phosphorylation of I kappa B alpha precedes but is not sufficient for its dissociation from NF-kappa B. Mol. Cell. Biol. 15: 1302.
17. FINCO, T. S., A. A. BEG, and A. S. BALDWIN. 1994. Inducible phosphorylation of I kappa B alpha is not sufficient for its dissociation from NF-kappa B and is inhibited by protease inhibitors. Proc. Natl. Acad. Sci. USA 91: 11884.
18. LIN, Y. C., K. BROWN, and U. SIEBENLIST. 1995. Activation of NF-kappa B required proteolysis of the inhibitor I kappa B alpha: signal-induced phosphorylation of I kappa B alpha alone does not release active NF-kappa B. Proc. Natl. Acad. Sci. USA 92: 552.
19. MIYAMOTO, S., M. MAKI, M. J. SCHMITT, M. HATANAKA, and I. M. VERMA. 1994. Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B. Proc. Natl. Acad. Sci. USA 91: 12740.
20. PALOMBELLA, V. J., O. J. RANDO, A. L. GOLDBERG, and T. MANIATIS. 1994. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78: 773.
21. TRAENCKNER, E. B. M., S. WILK, and P. A. BAEUERLE. 1994. A proteasome inhibitor prevents activation of NF-kappa B alpha that is still bound to NF-kappa B. EMBO J. 13: 5433.
22. BROCKMAN, J. A., D. C. SCHERER, T. A. MCKINSEY, S. M. HALL, X. X. QI, W. Y. LEE, and D. W. BALLARD. 1995. Coupling of a signal response domain in I kappa B alpha to multiple pathway for NF-kappa B activation. Mol. Cell. Biol. 15: 2809.
23. BROWN, K., S. GERSTBERGER, L. CARLSON, G. FRANZOSO. and U. SEIBENLIST. 1995. Control of I kappa B alpha proteolysis by site-specific, signal induced phosphorylation. Science 267: 1485.
24. RODRIGUEZ, M. S., I. MICHALOPOULOS, F. ARENZANASEISEDDOS, and R. T. HAY. 1995. Inducible degradation of I kappa B alpha in vitro and in vivo requires the acidic C-terminal domain of the protein. Mol. Cell. Biol. 15: 2413.
25. TRAENCKNER, E. B. M., H. L. PAHL, T. HENKEL, K. N. SCHMIDT, S. WILK, and P. A. BAEUERLE. 1995. Phosphorylation of human I kappa B alpha on serines 32 and 36 controls I kappa B alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBO J. 14: 2876.
26. SUN, S.-C., J. ELWOOD, and W. C. GREENE. 1996. Both Amino- and Carboxyl-terminal sequences within I kappa B alpha regulate its inducible degradation. Mol. Cell. Biol. 16: 1058.
27. CHEN, Z., J. HAGLER, V. J. PALOMBELLA, F. MELANDRI, D. SCHERER, D. BALLARD, and T. MANIATIS. 1995. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes and Dev. 9: 1586.
28. BALDI, L. K. BROWN, G. FRANZOSO, and U. SIEBENLIST. 1996. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B alpha. J. Biol. Chem. 271: 376.
29. VAN ANTWERP, D. J., and I. M. VERMA. 1996. Signal-induced degradation of I kappa B alpha: association with NF-kappa B and PEST sequence in I kappa B alpha are not required. Mol. Cell. Biol.16: 6037.
30. SUYANG, H. R. PHILLIPS, I. DOUGLAS, and S. GHOSH. 1996. Role unphosphorylated, newly synthetized I kappa B beta persistent activation of NF kappa B. Mol. Cell. Biol. 16: 5444.
31. WEIL, R., C. LAURENT-WINTER, and A. ISRAËL. 1997. Regulation of I kappa B beta degradation: similarities and differences with I kappa B alpha. J. Biol. Chem. In press.
32. LIN, Y. C., K. BROWN, and U. SIEBENLIST. 1995. Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B alpha: signal-induced phosphorylation of I kappa B alpha alone does not release active NF-kappa B. Proc. Natl. Acad. Sci. USA 92: 552.
33. BROWN, K., S. PARK, T. KANNO, G. FRANZOSO, and U. SIEBENLIST. 1993. Mutual Regulation of the Transcriptional Activator NF-kappa B and its inhibitor, I kappa B alpha. Proc. Natl. Acad. Sci. USA 90: 2532.
34. BEG, A. A., T. S. FINCO, P. V. NANTERMET, and A. J. BALDWIN. 1993. Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I kappa B alpha: a mechanism for NF-kappa B activation. Mol. Cell. Biol. 13: 3301.
35. DIDONATO, J., F. MERCURIO, C. ROSETTE, J. WU-LI, H. SUYANG, S. GHOSH, and M. KARIN. 1996. Mapping the inducible I kappa B phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16: 1295.
36. MCKINSEY, T. A., J. A. BROCKMAN, D. C. SCHERER, S. W. AL-MURRANI, P. L. GREEN, and D. W. BALLARD. 1996. Inactivation of I kappa B beta by the tax protein of human T-cell leukemia virus type 1: a potential mechanism for constitutive induction of NF-kappa B. Mol. Cell. Biol. 16: 2083.
37. SCHEFFNER, M., J. M. HUIBREGTSE, R. D. VIERSTRA, and P. M. HOWLEY. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75: 495.
38. SCHEFFNER, M., J. M. HUIBREGTSE, A. J. LEVINE, and P. M. HOWLEY. 1990. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63: 1129.
39. AHN, J. Y., N. TANAHASHI, K. AKIYAMA, H. HISAMATSU, C. NODA, K. TANAKA, C. H. CHUNG, N. SHIBMARA, P. J. WILLY, J. D. MOTT, C. A. SLAUGHTER, and G. N. DE MARTINO. 1995. Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome. FEBS Lett. 366: 37.