The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for Iκb phosphorylation and NF-κB activation

Cell

Volumn 91, Issue 2, 1997, Pages 243-252

  Zandi, Ebrahim ^a   Rothwarf, David M ^a   Delhase, Mireille ^a   Hayakawa, Makio ^a   Karin, Michael ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LEUCINE ZIPPER PROTEIN; PROTEIN KINASE; CHUK PROTEIN, HUMAN; I KAPPA B KINASE; IKBKB PROTEIN, HUMAN; IKBKE PROTEIN, HUMAN; PROTEIN SERINE THREONINE KINASE; TRANSCRIPTION FACTOR RELA;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PHOSPHORYLATION; ENZYME PURIFICATION; ENZYME SUBUNIT; HELA CELL; HUMAN; HUMAN CELL; MOLECULAR CLONING; PRIORITY JOURNAL; AMINO ACID SEQUENCE; CELL NUCLEUS; CHEMISTRY; ENZYME ACTIVATION; GENETICS; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION;

AMINO ACID SEQUENCE; CELL NUCLEUS; CLONING, MOLECULAR; ENZYME ACTIVATION; HELA CELLS; HELIX-TURN-HELIX MOTIFS; HUMANS; I-KAPPA B KINASE; LEUCINE ZIPPERS; MOLECULAR SEQUENCE DATA; NF-KAPPA B; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; TRANSCRIPTION FACTOR RELA;

EID: 0030613551     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80406-7     Document Type: Article

References (28)

1. Alkalay, I., Yaron, A., Hatzubai, A., Jung, S., Avraham, A., Gerlitz, O., Pashut-Lavon, I., and Ben-Neriah, Y. (1995). In vivo stimulation of IκB phosphorylation is not sufficient to activate NF-κB. Mol. Cell. Biol. 15, 1294-1301.
2. Baeuerle, P.A., and Baltimore, D. (1996). NF-κB: ten years after. Cell 87, 13-20.
3. Baeuerle, P.A., and Henkel, T. (1994). Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12, 141-179.
4. Baldwin, A.S. (1996). The NF-κB and I-κB proteins: new discoveries and insights. Annu. Rev. Immunol. 14, 649-681.
5. Barnes, P.J., and Karin, M. (1997). Nuclear factor-κB - A pivotal transcription factor in chronic inflammatory diseases. New Engl. J. Med. 336, 1066-1071.
6. Beg, A.A., and Baldwin, A.S., Jr. (1993). The IκB proteins: multifunctional regulators of Rel/NF-κB transcription factors. Genes Dev. 7, 2064-2070.
7. Beg, A.A., and Baltimore, D. (1996). An essential role for NF-κB in preventing TNF-α-induced cell death. Science 274, 782-784.
8. Brockman, J.A., Scherer, D.C., McKinsey, T.A., Hall, S.M., Qi, X., Lee, W.Y., and Ballard, D.W. (1995). Coupling of a signal response domain in IκB to multiple pathways for NF-κB activation. Mol. Cell. Biol. 15, 2809-2818.
9. Brown, K., Gerstberger, S., Carlson, L., Franzoso, G., and Siebenlist, U. (1995). Control of IκBα proteolysis by site-specific, signal-induced phosphorylation. Science 267, 1485-1491.
10. Chen, Z., Hagler, J., Palombella, V.J., Melandri, F., Scherer, D., Ballard, D., and Maniatis, T. (1995). Signal-induced site-specific phosphorylation targets IκB to the ubiquitin-proteasome pathway. Genes Dev. 9, 1586-1597.
11. Chen, Z.J., Parent, L., and Maniatis, T. (1996). Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell 84, 853-862.
12. Connelly, M.A., and Marcu, K.B. (1995). CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain. Cell Mol. Biol. Res. 41, 537-549.
13. DiDonato, J.A., Hayakawa, M., Rothwarf, D.M., Zandi, E., and Karin, M. (1997). A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388, 548-554.
14. DiDonato, J.A., Mercurio, F., and Karin, M. (1995). Phosphorylation of IκBα precedes but is not sufficient for its dissociation from NF-κB. Mol. Cell. Biol. 15, 1302-1311.
15. DiDonato, J.A., Mercurio, F., Rosette, C., Wu-li, J., Suyang, H., Ghosh, S., and Karin, M. (1996). Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16, 1295-1304.
16. Gilmore, T.D., and Morin, P.J. (1993). The IκB proteins: members of a multifunctional family. Trends Genet. 9, 427-433.
17. Hsu, H., Shu, B.H., Pan, M.G., and Goeddel, D.V. (1996). TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84, 299-308.
18. Lee, F.S., Hagler, J., Chen, Z.J., and Maniatis, T. (1997). Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell 88, 213-222.
19. Liu, Z.-G., Hu, H., Goeddel, D.V., and Karin, M. (1996). Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis, while NF-κB activation prevents cell death. Cell 87, 565-576.
20. Malinin, N.L, Boldin, M.P., Kovalenko, A.V., and Wallach, D. (1997). MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature 385, 540-544.
21. Morgan, D.O. (1995). Principles of CDK regulation. Nature 374, 131-134.
22. Régnier, C.H., Yeong Song, H., Gao, X., Goeddel, D.V., Cao, Z., and Rothe, M.(1997). Identification and characterization of an IκB kinase. Cell 90, 373-383.
23. Taylor, S.S., Knighton, D.R., Zheng, J., Ten Eyck, L.F., and Sowadski, J.M. (1992). Structural framework for the protein kinase family. Annu. Rev. Cell Biol. 8, 429-462.
24. Traenckner, E.B., Pahl, H.L, Henkel, T., Schmidt, K.N., Wilk, S., and Baeuerle, P.A. (1995). Phosphorylation of human IκB on serines 32 and 36 controls IκB proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14, 2876-2883.
25. Van Antwerp, D.J., Martin, S.J., Kafri, T., Green, D.R., and Verma, I.M. (1996). Suppression of TNF-α-induced apoptosis by NF-κB. Science 274, 787-789.
26. Verma, I.M., Stevenson, J.K., Schwarz, E.M., Van Antwerp, D., and Miyamoto, S. (1995). Rel/NF-κB/IκB family: intimate tales of association and dissociation. Genes Dev. 9, 2723-2735.
27. Wang, C.-Y., Mayo, M.W., and Baldwin, A.S., Jr. (1996). TNF-and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. Science 274, 784-787.
28. Whiteside, T., Ernst, M.K., LeBail, O., Laurent-Winter, C., Rice, N., and Israel, A. (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.