Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation

Molecular and Cellular Biology

Volumn 16, Issue 4, 1996, Pages 1295-1304

  DiDonato, Joseph ^a   Mercurio, Frank ^b   Rosette, Caridad ^a   Wu Li, Jian ^b   Suyang, Helena ^c   Ghosh, Sankar ^c   Karin, Michael ^a  

^a San Diego   (United States)

^b Signal Pharmaceuticals   (United States)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; PHORBOL ESTER; TUMOR NECROSIS FACTOR; CHUK PROTEIN, HUMAN; CHUK PROTEIN, MOUSE; DNA BINDING PROTEIN; I KAPPA B; I KAPPA B BETA; I KAPPA B KINASE; IKBKB PROTEIN, HUMAN; IKBKB PROTEIN, MOUSE; IKBKE PROTEIN, HUMAN; IKBKE PROTEIN, MOUSE; LYSINE; NF KAPPAB INHIBITOR ALPHA; NF-KAPPAB INHIBITOR ALPHA; PROTEIN SERINE THREONINE KINASE; PROTEINASE INHIBITOR; SERINE; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN;

AMINO ACID ANALYSIS; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; HUMAN; HUMAN CELL; PEPTIDE MAPPING; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; ANIMAL; CELL STRAIN 3T3; DRUG ANTAGONISM; GENETICS; HELA CELL; METABOLISM; MOUSE; MUTATION; SERODIAGNOSIS;

3T3 CELLS; ANIMALS; DNA-BINDING PROTEINS; HELA CELLS; HUMANS; I-KAPPA B KINASE; I-KAPPA B PROTEINS; INTERLEUKIN-1; LYSINE; MICE; MUTATION; NF-KAPPA B; PEPTIDE MAPPING; PHOSPHORYLATION; PRECIPITIN TESTS; PROTEASE INHIBITORS; PROTEIN-SERINE-THREONINE KINASES; SERINE; TUMOR NECROSIS FACTOR-ALPHA; UBIQUITINS;

EID: 0029670083     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.4.1295     Document Type: Article

References (52)

1. raf-1. EMBO J. 13:1610-1619
2. Alkalay, I., A. Yaron, A. Hatzubai, S. Jung, A. Avraham, O. Gerlitz, I. Pashut-Lavon, and Y. Ben-Neriah. 1995. In vivo stimulation of IκB phosphorylation is not sufficient to activate NF-κB. Mol. Cell. Biol. 15:1294-1301.
3. 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 ubiquitin-proteasome pathway Proc Natl Acad. Sci. USA 92:10599-10603.
4. Baeuerle, P. A. 1991. The inducible transcriptional activator NF-κB. regulation by distinct protein subunits. Biochim. Biophys. Acta 1072:63-80.
5. Beg, A. A., and A. S. Baldwin, Jr. 1993. The IκB proteins: multifunctional regulators of Rel/NF-κB transcription factors Genes Dev. 7:2064-2070.
6. Beg, A. A., T. S. Finco, P. V. Nantermet, and A. Baldwin, Jr. 1993. Tumor necrosis factor and interleuktn-1 lead to phosphorylation and loss of IκBα: a mechanism for NF-κB activation. Mol. Cell. Biol. 13:3301-3310.
7. Blank, V., P. Kourilsky, and A. Israel. 1992. NF-κB and related proteins: Rel/dorsal homologies meet ankyrin-hke repeats. Trends Biochem. Sci. 17: 135-140.
8. Boyle, W. J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:110-149.
9. 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.
10. Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκBα-proteolysis by site-specific, signal-induced phosphorylation. Science 267:1485-1491.
11. Brown, K., S. Park, T. Kanno, G. Franzoso, and U. Siebenlist. 1993 Mutual regulation of the transcriptional activator NF-κB and its inhibitor, IκBα. Proc Natl. Acad. Sci. USA 90:2532-2536.
12. Chen, Z., 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
13. Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:1321.
14. Cordle, S. R., R. Donald, M. A. Read, and J. Hawiger. 1993 Lipopolysaccharide induces phosphorylatiors of MAD-3 and activation of c-Rel and related NF-κB proteins in human monocytic THP-1 cells. J. Biol. Chem. 268:11803-11810,
15. Devary, Y., C. Rosette, J. A. DiDonato, and M. Karin. 1993 NF-κB activation by ultraviolet light not dependent on a nuclear signal. Science 261:1442-1445.
16. DiDonato, J. A. Unpublished observations.
17. DiDonato, J. A., F. Mercurio, and M. Karin. 1995. Phosphorylation of IκBα precedes but is not sufficient for its dissociation from NF-κB Mol. Cell Biol. 15:1302-1311.
18. Finco, T. S., A. A. Beg, and A. S. Baldwin, Jr. 1994 Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors. Proc. Natl. Acad. Sci. USA 91:11884-11888.
19. Flotow, H., and P. J. Roach. 1991 Role of acidic residues as substrate determinants for casein kinase I. J. Biol. Chem 23:3724-3727.
20. Ghosh, S., and D. Baltimore. 1990 Activation in vivo of NF-κB by phosphorylation of its inhibitor IκB. Nature (London) 344:678-682.
21. Gilmore, T. D., and P. J. Morin. 1993 The IκB proteins: members of a multifunctional family. Trends Genet. 9:427-433.
22. Goldberg, A. L. 1992 The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur J. Biochem. 203:9-23.
23. Goldberg, A. L. 1995. Functions of the proteasome: the lysis at the end of the tunnel. Science 268:522-523
24. Grilli, M., J. J. Chiu, and M. J. Lenardo. 1993. NF-κB and Rel: participants in a multiform transcriptional regulatory system. Int. Rev. Cytol. 143:1-62.
25. Haas, A. L., and P. M. Bright. 1985. The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J Biol. Chem. 250:12464-12473.
26. Haskill, S., A. A. Beg, S. M. Tompkins, J. S. Morris, A. D. Yurochko, A. Sampson-Johannes, R. Mondal, P. Ralph, and A. Baldwin. Jr. 1991. Characterization of an immediate-early gene induced in adherent monocytes that encodes IκB-like activity Cell 65:1281-1289.
27. Helmberg, A., N. Auphan, C. Caelles, and M. Karin. 1995. Glucocorticoid-induced apoptosis of human leukemic cells is caused by the repressive function of the glucocorticoid receptor. EMBO J. 14:452-460
28. Henkel, T., T. Machleidt, I. Alkalay, M. Kronke, T. Ben-Neriah, and P. A. Baeuerle. 1993. Rapid proteolysis of IκBα is necessary for activation of transcription factor NF-κB Nature (London) 365:182-185.
29. Hershko, A., and A. Ciechanover. 1992. The ubiquitin system for protein degradation Annu. Rev Biochem. 61:761-807.
30. Kemp, B. E., D. J. Graves, E. Benjamini, and E. G. Krebs. 1977. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase. J. Biol. Chem 252:4888-4894.
31. Kumar, A., J. Haque, J. Lacoste, J. Hiscott, and B. R. G. Williams. 1994. Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB. Proc. Natl. Acad. Sci. USA 91:6288-6292
32. Li, S., and J. M. Sedivy. 1993. Raf-1 protein kinase activates the NF-κB transcription factor by dissociating the cytoplasmic NF-κB-IκB complex. Proc. Natl Acad. Sci. USA 90:9247-9251.
33. Lin, Y.-C., K. Brown, and U. Siebenlist. 1995. Activation of NFκB requires proteolysis of the inhibitor IκBα. signal-induced phosphorylation of IκBα alone does not release active NF-κB. Proc. Natl. Acad. Sci. USA 92:3003-3009.
34. Liou, H. C., and D. Baltimore. 1993. Regulation of the NF-κB/Rel transcription factor and IκB inhibitor system. Curr. Opin. Cell Biol. 5:477-487.
35. Mellits, K. D., R. T. Hay, and S. Goodbourn. 1993. Proteolytic degradation of MAD-3 (IκBα) and enhanced processing of the NF-κB precursor p105 are obligatory steps in the activation of NF-κB. Nucleic Acids Res. 21:5059-5066.
36. Mercurio, F., J. DiDonato, C. Rosette, and M. Karin. 1992. Molecular cloning and characterization of a novel Rel/NFκB family member displays structural and functional homology to NF-κB p50/-105 DNA Cell Biol. 11:523-537
37. Mercurio, F., J. A. DiDonato, C. Rosette, and M. Karin. 1993. p105 and p98 precursor proteins play an active role in NF-κB mediated signal transduction. Genes Dev. 7:705-718.
38. Minden, A., A. Lin, M. McMahon, C. Lange-Carter, B. Dérijard, R. J. Davis, G. L. Johnson, and M. Karin. 1994. Differential activation of ERK and JNK MAP kinases by Raf-1 and MEKK. Science 266:1719-1723.
39. Miyamoto, S., M. Maki, M. J. Schmitt, M. Hatanaka, and I. M. Verma. 1994. Tumor necrosis factor α-induced phosphorylation of IκBα is a signal for its degradation but not dissociation from NF-κB. Proc. Natl. Acad. Sci. USA 91:12740-12744.
40. Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-κB precursor and the activation of NF-κB. Cell 78:773-785.
41. Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
42. Sen, R., and D. Baltimore. 1986. Inducibility of the κ immunoglobulin enhancer-binding protein NF-κB by a posttranslational mechanism. Cell 47: 921-928.
43. Siebenlist, U., G. Franzoso, and K. Brown. 1994. Structure, regulation and function of NF-κB. Annu. Rev. Cell Biol. 10:405-455.
44. Thanos, D., and T. Maniatis. 1995. NF-κB: a lesson in family values Cell 80:529-532.
45. Thompson, J. E., R. J. Philips, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1995 IκBβ regulates the persistent response in a biphasic activation of NF-κB Cell 80:573-582.
46. Traenckner, E. B., H. L. Pahl, T. Henkel, K. N. 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.
47. Traenckner, E. B.-M., S. Wilk, and P. A. Baeuerle. 1994. A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκBα that is still bound to NF-κB. EMBO J. 13:5433-5441.
48. Treier, M., L. M. Staszewski, and D. Bhomann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain. Cell 78:787-798.
49. Tuazon, P. T., and J. A. Traugh. 1991 Casein kinase I and II - multipotential serine protein kinases: structure, function and regulation. Adv. Second Messenger Phosphoprotein Res. 23:123-164.
50. Vinitsky, A., C. Michaud, J. C. Powers, and M. Orlowski. 1992 Inhibition of the chymotrypsin-like activity of the pituitary proteinase complex. Biochemistry 31:9421-9428.
51. Whiteside, T., M. K. Ernst, O. LeBail, C. Laurent-Winter, N. Rice, and A. Israel. 1995. N- and C-terminal sequences control degradation of MAD3/ IκBα in response to inducers of NF-κB activity. Mol. Cell. Biol. 15:5339-5345.
52. Wilson, I. A., H. L. Niman, R. A. Houghten, A. R. Cherenson, M. L. Connolly, and R. A. Lerner. 1984. The structure of an antigenic determinant in a protein Cell 37:767-778.