NF-κB1 p105 negatively regulates TPL-2 MEK kinase activity

Molecular and Cellular Biology

Volumn 23, Issue 14, 2003, Pages 4739-4752

  Beinke, S ^a   Deka, J ^a   Lang, V ^a   Belich, M P ^a   Walker, P A ^a   Howell, S ^a   Smerdon, S J ^a   Gamblin, S J ^a   Ley, S C ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN P105; PROTEIN SERINE THREONINE KINASE; PROTEIN TPL2; UNCLASSIFIED DRUG; MAP2K1 PROTEIN, MOUSE; MAP3K8 PROTEIN, MOUSE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; ONCOPROTEIN; PEPTIDE FRAGMENT; PROTEIN PRECURSOR; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CARCINOGENICITY; CONTROLLED STUDY; ENZYME ACTIVITY; GENE DELETION; GENE MUTATION; MOLECULAR STABILITY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; STOICHIOMETRY; ANIMAL; BINDING SITE; CELL STRAIN 3T3; ENZYME STABILITY; GENETICS; METABOLISM; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

ANIMALIA;

3T3 CELLS; ANIMALS; BINDING SITES; ENZYME STABILITY; MAP KINASE KINASE 1; MAP KINASE KINASE KINASES; MICE; MITOGEN-ACTIVATED PROTEIN KINASE KINASES; NF-KAPPA B; NF-KAPPA B P50 SUBUNIT; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN PRECURSORS; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; PROTO-ONCOGENE PROTEINS; RECOMBINANT PROTEINS;

EID: 0038112098     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.14.4739-4752.2003     Document Type: Article

References (34)

1. Aoki, M., F. Hamada, T. Sugimoto, S. Sumida, T. Akiyama, and K. Toyoshima. 1993. The human cot proto-oncogene encodes two protein serine/threonine kinases with different transforming activities by alternative initiation of translation. J. Biol. Chem. 268:22723-22732.
2. Beinke, S., M. P. Belich, and S. C. Ley. 2002. The death domain of NF-κB1 p105 is essential for signal-induced p105 proteolysis. J. Biol. Chem. 277: 24162-24168.
3. Belich, M. P., A. Salmeron, L. H. Johnston, and S. C. Ley. 1999. TPL-2 kinase regulates the proteolysis of the NF-κB inhibitory protein NF-κB1 p105. Nature 397:363-368.
4. Ceci, J. D., C. P. Patriotis, C. Tsatsanis, A. M. Makris, R. Kovatch, D. A. Swing, N. A. Jenkins, P. N. Tsichlis, and N. G. Copeland. 1997. TPL-2 is an oncogenic kinase that is activated by carboxy-terminal truncation. Gene Dev. 11:688-700.
5. Chan, A. M.-L., M. Chedid, E. S. McGovern, N. C. Popescu, T. Miki, and S. A. Aaronson. 1993. Expression cDNA cloning of a serine kinase transforming gene. Oncogene 8:1329-1333.
6. Chlariello, M., M. J. Marinissen, and J. S. Gutkind. 2000. Multiple mitogen-activated protein kinase signaling pathways connect the Cot oncoprotein to the c-Jun promoter and to cellular transformation. Mol. Cell. Biol. 20:1747-1758.
7. Cowley, S., H. Paterson, P. Kemp, and C. J. Marshall. 1994. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell 77:841-852.
8. Delhase, M., M. Hayakawa, Y. Chen, and M. Karin. 1999. Positive and negative regulation of IκB kinase activity through IKK-β subunit phosphorylation. Science 284:309-313.
9. Donald, R., D. W. Ballard, and J. Hawiger. 1995. Proteolytic processing of NF-κB/1κB in human monocytes. J. Biol. Chem. 270:9-12.
10. Dumitru, C. D., J. D. Ceci, C. Tsatsanis, D. Kontoyiannis, K. Stamatakis, J.-H. Lin, C. Patriotis, N. A. Jenkins, N. G. Copeland, G. Kollias, and P. N. Tsichlis. 2000. TNFα induction by LPS is regulated posttranscriptionally via a TPL2/ERK-dependent pathway. Cell 103:1071-1083.
11. Gerondakis, S., N. Morrice, I. B. Richardson, R. Wettenhall, J. Fecondo, and R. J. Grumont. 1993. The activity of a 70-kDa IκB molecule identical to the carboxyl terminus of the p105 NF-κB precursor is modulated by protein kinase A. Cell Growth Differ. 4:617-627.
12. Heissmeyer, V., D. Krappmann, F. G. Wulczyn, and C. Scheidereit. 1999. NF-κB p105 is a target on IκB kinases and controls signal induction of BCL-3-p50 complexes. EMBO J. 18:4766-4788.
13. Henkel, T., U. Zabel, K. van Zee, J. M. Muller, E. Fanning, and P. A. Baeuerle. 1992. Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit. Cell 68: 1121-1133.
14. Huxford, T., D. B. Huang, S. Malek, and G. Ghosh. 1998. The crystal structure of the IκBα-/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell 95:759-770.
15. Ishikawa, H., E. Claudio, D. Dambach, C. Raventos-Suarez, C. Ryan, and R. Bravo. 1998. Chronic inflammation and susceptibility to bacterial infections in mice lacking the polypeptide (p) 105 precursor (NF-κB1) but expressing p50. J. Exp. Med. 187:985-996.
16. Jacobs, M. D., and S. C. Harrison. 1998. Structure of an IκBα/NF-κB complex. Cell 95:749-758.
17. Kabouridis, P. S., A. I. Magee, and S. C. Ley. 1997. S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J. 16:4983-4998.
18. Karin, M., and Y. Ben-Neriah. 2000. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18:621-663.
19. Lang, V., J. Janzen, G. Z. Fischer, Y. Soneji, S. Beinke, A. Salmeron, H. Allen, R. T. Hay, Y. Ben-Neriah, and S. C. Ley. 2003. βTrCP-mediated proteolysis of NF-κB1 p105 requires phosphorylation of p105 serines 927 and 932. Mol. Cell. Biol. 23:402-413.
20. Leevers, S. J., H. F. Paterson, and C. J. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targetting Raf to the plasma membrane. Nature 369:411-414.
21. Lin, X., E. T. Cunningham, Y. Mu, R. Geleziunas, and W. C. Greene. 1999. The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-κB acting through the NF-κB-inducing kinase and IκB kinases. Immunity 10:271-280.
22. Lund, A. H., G. Turner, A. Trubetskoy, E. Verhoeven, E. Wientjens, D. Hulsman, R. Russell, R. A. DePinho, J. Lenz, and M. van Lohuizen. 2002. Genome-wide retroviral insertional tagging of genes involved in cancer in Cdkn2a-deficient mice. Nat. Gene 32:160-165.
23. Makris, A., C. Patriotis, S. E. Bear, and P. N. Tsichlis. 1993. Genomic organization and expression of Tpl-2 in normal cells and moloney murine leukemia virus-induced rat T-cell lymphomas: activation by provirus insertion. J. Virol. 67:4283-4289.
24. Mikkers, H., J. Allen, P. Knipscheer, L. Romeyn, A. Hart, E. Vink, and A. Berns. 2002. High throughput retroviral tagging to identify components of specific signaling pathways in cancer. Nat. Gene 32:153-159.
25. Patriotis, C., A. Makris, S. E. Bear, and P. N. Tsichlis. 1993. Tumor progression locus 2 (Tpl-2) encodes a protein kinase involved in the progression of rodent T-cell lymphomas and in T-cell activation. Proc. Natl. Acad. Sci. USA 90:2251-2255.
26. Patriotis, C., A. Makris, J. Chernoff, and P. N. Tsichlis. 1994. Tpl-2 acts in concert with Ras and Raf-1 to activate mitogen-activated protein kinase. Proc. Natl. Acad. Sci. USA 91:9755-9759.
27. Salmeron, A., T. B. Ahmad, G. W. Carlile, D. Pappin, R. P. Narsimhan, and S. C. Ley. 1996. Activation of MEK-1 and SEK-1 by Tpl-2 proto-oncoprotein, a novel MAP kinase kinase kinase. EMBO J. 15:817-826.
28. Salmeron, A., J. Janzen, Y. Soneji, N. Bump, J. Kamens, H. Allen, and S. C. Ley. 2001. Direct phosphorylation of NF-κB p105 by the IκB kinase complex on serine 927 is essential for signal-induced p105 proteolysis. J. Biol. Chem. 276:22215-22222.
29. Sha, W. C., H.-C. Liou, E. I. Tuomanen, and D. Baltimore. 1995. Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses. Cell 80:321-330.
30. Siebenlist, U., G. Franzoso, and K. Brown. 1994. Structure, regulation and function of NF-κB. Annu. Rev. Cell Biol. 10:405-455.
31. Szabo, A., L. Stolz, and R. Granzow. 1995. Surface plasmon resonance and its use in biomolecular interaction analysis (BIA). Curr. Opin. Struct. Biol. 5:699-705.
32. Waterfield, M. R., M. Zhang, L. P. Norman, and S.-C. Sun. 2003. NF-κB1/p105 regulates lipopolysaccharide-stimulated MAP kinase signaling by governing the stability and function of the TPL-2 kinase. Mol. Cell 11:685-694.
33. Yeung, K. T., P. Janosch, B. McFerran, D. W. Rose, H. Mischak, J. M. Sedivy, and W. Kolch. 2000. Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the Raf kinase inhibitor protein. Mol. Cell. Biol. 20:3079-3085.
34. Yeung, K. T., T. Seitz, S. Li, P. Janosch, B. McFerran, C. Kaiser, F. Fee, K. D. Katsanakis, D. W. Rose, H. Mischak, J. M. Sedivy, and W. Kolch. 1999. Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature 401:173-177.