The COOH-terminal domain of wild-type Cot regulates its stability and kinase specific activity

Molecular and Cellular Biology

Volumn 23, Issue 20, 2003, Pages 7377-7390

  Gándara, Maria Luisa ^a   López, Pilar ^a   Hernando, Raquel ^a   Castaño, José G ^a   Alemany, Susana ^a,b  

^a UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

^b INSTITUTO DE INVESTIGACIONES BIOMÉDICAS ALBERTO SOLS   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COT PROTEIN; HYBRID PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; MUTANT PROTEIN; PROTEASOME; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CARCINOGENESIS; CELL ACTIVATION; CELL PROLIFERATION; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STABILITY; HALF LIFE TIME; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; ONCOGENE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN METABOLISM;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CELL LINE; CYSTEINE ENDOPEPTIDASES; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; MAP KINASE KINASE KINASES; MICE; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; NIH 3T3 CELLS; PLASMIDS; PRECIPITIN TESTS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SEQUENCE HOMOLOGY, AMINO ACID; TIME FACTORS; TRANSCRIPTION, GENETIC; TRANSFECTION;

ANIMALIA;

EID: 0141752770     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.20.7377-7390.2003     Document Type: Article

References (69)

1. Alessi, D. R., P. Cohen, A. Ashworth, S. Cowley, S. J. Leever, and C. J. Marshall. 1995. Assay and expression of mitogen-activated protein kinase, Map kinase kinase, and RAF. Methods Enzymol. 255:279-290.
2. Aoki, M., T. Akiyama, J. Miyoshi, and K. Toyoshima. 1991. Identification and characterization of protein products of the cot oncogene with serine kinase activity. Oncogene 6:1515-1519.
3. Arribas, J., P. Arizti, and J. G. Castano. 1994. Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex. J. Biol. Chem. 269:12858-12864.
4. Arribas, J., and J. G. Castano. 1993. A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. J. Biol. Chem. 268:21165-21171.
5. Arribas, J., and J. G. Castano. 1990. Kinetic studies of the differential effect of detergents on the peptidase activities of the multicatalytic proteinase from rat liver. J. Biol. Chem. 265:13969-13973.
6. Ballester, A., R. Tobena, C. Lisbona, V. Calvo, and S. Alemany. 1997. Cot kinase regulation of IL-2 production in Jurkat T cells. J. Immunol. 159:1613-1618.
7. Ballester, A., A. Velasco, R. Tobena, and S. Alemany. 1998. Cot kinase activates tumor necrosis factor-alpha gene expression in a cyclosporin A-resistant manner. J. Biol. Chem. 273:14099-14106.
8. 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.
9. Blair, D. G., M. K. Oskarsson, A. Seth, K. J. Dunn, M. Dean, M. Zweig, M. A. Tainsky, and G. F. Vande Woude. 1986. Analysis of the transforming potential of the human homolog of mos. Cell 46:785-794.
10. Bonner, T. I., H. Oppermann, P. Seeburg, S. B. Kerby, M. A. Gunnell, A. C. Young, and U. R. Rapp. 1986. The complete coding sequence of the human raf oncogene and the corresponding structure of the c-raf-1 gene. Nucleic Acids Res. 14:1009-1015.
11. 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. Genes Dev. 11:688-700.
12. Chan, A. M., 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.
13. Chiariello, 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.
14. Ciechanover, A., A. Orian, and A. L. Schwartz. 2000. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 22:442-451.
15. Coffino, P. 2001. Regulation of cellular polyamines by antizyme. Nat. Rev. Mol. Cell Biol. 2:188-194.
16. Corish, P., and C. Tyler-Smith. 1999. Attenuation of green fluorescent protein half-life in mammalian cells. Protein Eng. 12:1035-1040.
17. de Gregorio, R., M. A. Iniguez, M. Fresno, and S. Alemany. 2001. Cot kinase induces cyclooxygenase-2 expression in T cells through activation of the nuclear factor of activated T cells. J. Biol. Chem. 276:27003-27009.
18. Dent, P., W. Haser, T. A. Haystead, L. A. Vincent, T. M. Roberts, and T. W. Sturgill. 1992. Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro. Science 257:1404-1407.
19. Dufner, A., M. Andjelkovic, B. M. Burgering, B. A. Hemmings, and G. Thomas. 1999. Protein kinase B localization and activation differentially affect S6 kinase 1 activity and eukaryotic translation initiation factor 4E-binding protein 1 phosphorylation. Mol. Cell. Biol. 19:4525-4534.
20. 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. TNF-alpha induction by LPS is regulated posttranscriptionally via a Tpl2/ERK-dependent pathway. Cell 103:1071-1083.
21. Eliopoulos, A. G., C. Davies, S. S. Blake, P. Murray, S. Najafipour, P. N. Tsichlis, and L. S. Young. 2002. The oncogenic protein kinase Tpl-2/Cot contributes to Epstein-Barr virus-encoded latent infection membrane protein 1-induced NF-κB signaling downstream of TRAF2. J. Virol. 76:4567-4579.
22. Eliopoulos, A. G., C. D. Dumitru, C. C. Wang, J. Cho, and P. N. Tsichlis. 2002. Induction of COX-2 by LPS in macrophages is regulated by Tpl2-dependent CREB activation signals. EMBO J. 21:4831-4840.
23. Erny, K. M., J. Peli, J. F. Lambert, V. Muller, and H. Diggelmann. 1996. Involvement of the Tpl-2/cot oncogene in MMTV tumorigenesis. Oncogene 13:2015-2020.
24. Glotzer, M., A. W. Murray, and M. W. Kirschner. 1991. Cyclin is degraded by the ubiquitin pathway. Nature 349:132-138.
25. Hagemann, D., J. Troppmair, and U. R. Rapp. 1999. Cot proto-oncoprotein activates the dual specificity kinases MEK-1 and SEK-1 and induces differentiation of PC12 cells. Oncogene 18:1391-1400.
26. Heidecker, G., M. Huleihel, J. L. Cleveland, W. Kolch, T. W. Beck, P. Lloyd, T. Pawson, and U. R. Rapp. 1990. Mutational activation of c-raf-1 and definition of the minimal transforming sequence. Mol. Cell. Biol. 10:2503-2512.
27. Henchoz, S., Y. Chi, B. Catarin, I. Herskowitz, R. J. Deshaies, and M. Peter. 1997. Phosphorylation- and ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor Far1p in budding yeast. Genes Dev. 11:3046-3060.
28. Hershko, A., and A. Ciechanover. 1998. The ubiquitin system. Annu. Rev. Biochem. 67:425-479.
29. Hochstrasser, M., and A. Varshavsky. 1990. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell 61:697-708.
30. Howe, L. R., S. J. Leevers, N. Gomez, S. Nakielny, P. Cohen, and C. J. Marshall. 1992. Activation of the MAP kinase pathway by the protein kinase raf. Cell 71:335-342.
31. Kane, L. P., M. N. Mollenauer, Z. Xu, C. W. Turck, and A. Weiss. 2002. Akt-dependent phosphorylation specifically regulates Cot induction of NF-κB-dependent transcription. Mol. Cell. Biol. 22:5962-5974.
32. King, R. W., R. J. Deshaies, J. M. Peters, and M. W. Kirschner. 1996. How proteolysis drives the cell cycle. Science 274:1652-1659.
33. King, R. W., M. Glotzer, and M. W. Kirschner. 1996. Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates. Mol. Biol. Cell 7:1343-1357.
34. Kornitzer, D., and A. Ciechanover. 2000. Modes of regulation of ubiquitin-mediated protein degradation. J. Cell Physiol. 182:1-11.
35. Krappmann, D., F. G. Wulczyn, and C. Scheidereit. 1996. Different mechanisms control signal-induced degradation and basal turnover of the NF-κB inhibitor IκBα in vivo. EMBO J. 15:6716-6726.
36. Kroll, M., M. Conconi, M. J. Desterro, A. Marin, D. Thomas, B. Friguet, R. T. Hay, J. L. Virelizier, F. Arenzana-Seisdedos, and M. S. Rodriguez. 1997. The carboxy-terminus of IκBα determines susceptibility to degradation by the catalytic core of the proteasome. Oncogene 15:1841-1850.
37. Kyriakis, J. M., H. App, X. F. Zhang, P. Banerjee, D. L. Brautigan, U. R. Rapp, and J. Avruch. 1992. Raf-1 activates MAP kinase-kinase. Nature 358:417-421.
38. Lin, X., E. T. Cunningham, Jr., 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.
39. Lucas, J., D. Lobo, E. Terry, E. L. Hogan, and N. L. Banik. 1992. Susceptibility of myelin proteins to a neutral endoproteinase: the degradation of myelin basic protein (MBP) and P2 protein by purified bovine brain multicatalytic proteinase complex (MPC). Neurochem. Res. 17:1261-1266.
40. 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.
41. Mansour, S. J., W. T. Matten, A. S. Hermann, J. M. Candia, S. Rong, K. Fukasawa, G. F. Vande Woude, and N. G. Ahn. 1994. Transformation of mammalian cells by constitutively active MAP kinase kinase. Science 265:966-970.
42. Miyoshi, J., T. Higashi, H. Mukai, T. Ohuchi, and T. Kakunaga. 1991. Structure and transforming potential of the human cot oncogene encoding a putative protein kinase. Mol. Cell. Biol. 11:4088-4096.
43. Nebreda, A. R., C. Hill, N. Gomez, P. Cohen, and T. Hunt. 1993. The protein kinase mos activates MAP kinase kinase in vitro and stimulates the MAP kinase pathway in mammalian somatic cells in vivo. FEBS Lett. 333:183-187.
44. Nieto, A., E. Mira, and J. G. Castano. 1990. Transcriptional regulation of rat liver protein disulphide-isomerase gene by insulin and in diabetes. Biochem. J. 267:317-323.
45. Nishizawa, M., N. Furuno, K. Okazaki, H. Tanaka, Y. Ogawa, and N. Sagata. 1993. Degradation of Mos by the N-terminal proline (Pro2)-dependent ubiquitin pathway on fertilization of Xenopus eggs: possible significance of natural selection for Pro2 in Mos. EMBO J. 12:4021-4027.
46. 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.
47. 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.
48. Patschinsky, T., and K. Bister. 1988. Structural analysis of normal and transforming mil(raf) proteins: effect of 5′-truncation on phosphorylation in vivo or in vitro. Oncogene 3:357-364.
49. Patschinsky, T., H. W. Jansen, H. Blocker, R. Frank, and K. Bister. 1986. Structure and transforming function of transduced mutant alleles of the chicken c-myc gene. J. Virol. 59:341-353.
50. Pereira, M. E., T. Nguyen, B. J. Wagner, J. W. Margolis, B. Yu, and S. Wilk. 1992. 3,4-Dichloroisocoumarin-induced activation of the degradation of beta-casein by the bovine pituitary multicatalytic proteinase complex. J. Biol. Chem. 267:7949-7955.
51. Posada, J., N. Yew, N. G. Ahn, G. F. Vande Woude, and J. A. Cooper. 1993. Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro. Mol. Cell. Biol. 13:2546-2553.
52. Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
53. 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.
54. Sanchez-Gongora, E., C. Lisbona, R. de Gregorio, A. Ballester, V. Calvo, L. Perez-Jurado, and S. Alemany. 2000. COT kinase proto-oncogene expression in T cells: implication of the JNK/SAPK signal transduction pathway in COT promoter activation. J. Biol. Chem. 275:31379-31386.
55. Schutte, J., J. Viallet, M. Nau, S. Segal, J. Fedorko, and J. Minna. 1989. jun-B inhibits and c-fos stimulates the transforming and trans-activating activities of c-jun. Cell 59:987-997.
56. Sheng, J., A. Kumagai, W. G. Dunphy, and A. Varshavsky. 2002. Dissection of c-MOS degron. EMBO J. 21:6061-6071.
57. Shibuya, E. K., and J. V. Ruderman. 1993. Mos induces the in vitro activation of mitogen-activated protein kinases in lysates of frog oocytes and mammalian somatic cells. Mol. Biol. Cell 4:781-790.
58. Sourvinos, G., C. Tsatsanis, and D. A. Spandidos. 1999. Overexpression of the Tpl-2/Cot oncogene in human breast cancer. Oncogene 18:4968-4973.
59. Stancovski, I., H. Gonen, A. Orian, A. L. Schwartz, and A. Ciechanover. 1995. Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes. Mol. Cell. Biol. 15:7106-7116.
60. Touitou, R., J. Richardson, S. Bose, M. Nakanishi, J. Rivett, and M. J. Allday. 2001. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. EMBO J. 20:2367-2375.
61. Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78:787-798.
62. Tsatsanis, C., C. Patriotis, S. E. Bear, and P. N. Tsichlis. 1998. The Tpl-2 proto-oncoprotein activates the nuclear factor of activated T cells and induces interleukin 2 expression in T cell lines. Proc. Natl. Acad. Sci. USA 95:3827-3832.
63. Tsatsanis, C., C. Patriotis, and P. N. Tsichlis. 1998. Tpl-2 induces IL-2 expression in T-cell lines by triggering multiple signaling pathways that activate NFAT and NF-κB. Oncogene 17:2609-2618.
64. Varshavsky, A. 1991. Naming a targeting signal. Cell 64:13-15.
65. 1 phase progression in T cells. J. Immunol. 166:6084-6090.
66. Verma, R., and R. J. Deshaies. 2000. A proteasome howdunit: the case of the missing signal. Cell 101:341-344.
67. Verma, R., H. McDonald, J. R. Yates III, and R. J. Deshaies. 2001. Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk. Mol. Cell 8:439-448.
68. Voges, D., P. Zwickl, and W. Baumeister. 1999. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1015-1068.
69. Wood, T. G., M. L. McGeady, B. M. Baroudy, D. G. Blair, and G. F. Vande Woude. 1984. Mouse c-mos oncogene activation is prevented by upstream sequences. Proc. Natl. Acad. Sci. USA 81:7817-7821.