메뉴 건너뛰기




Volumn 288, Issue 2, 2013, Pages 819-825

The dual-specificity phosphatase DUSP14 negatively regulates tumor necrosis factor- and interleukin-1-induced nuclear factor-κB activation by dephosphorylating the protein kinase TAK1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION LOOPS; ACTIVATION PATHWAY; INFLAMMATORY RESPONSE; NEGATIVE REGULATORS; NUCLEAR FACTORS; OVER-EXPRESSION; PROINFLAMMATORY CYTOKINES; PROTEIN KINASE; REGULATORY MECHANISM; TUMOR NECROSIS FACTORS;

EID: 84872358122     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.412643     Document Type: Article
Times cited : (45)

References (23)
  • 2
    • 79651473582 scopus 로고    scopus 로고
    • NF-κB in immunobiology
    • Hayden, M. S., and Ghosh, S. (2011) NF-κB in immunobiology. Cell Res. 21, 223-244
    • (2011) Cell Res. , vol.21 , pp. 223-244
    • Hayden, M.S.1    Ghosh, S.2
  • 3
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-κB transcription factors in the immune system
    • Vallabhapurapu, S., and Karin, M. (2009) Regulation and function of NF-κB transcription factors in the immune system. Annu. Rev. Immunol. 27, 693-733
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 5
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-IκB as well as the MAP kinase cascade in the IL-1 signalling pathway
    • Ninomiya-Tsuji, J., Kishimoto, K., Hiyama, A., Inoue, J., Cao, Z., and Matsumoto, K. (1999) The kinase TAK1 can activate the NIK-IκB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature 398, 252-256
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5    Matsumoto, K.6
  • 6
    • 0029551805 scopus 로고
    • Identification of a member of the MAPKKK family as a potential Mediator of TGF-β signal transduction
    • Yamaguchi, K., Shirakabe, K., Shibuya, H., Irie, K., Oishi, I., Ueno, N., Taniguchi, T., Nishida, E., and Matsumoto, K. (1995) Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction. Science 270, 2008-2011 (Pubitemid 26097194)
    • (1995) Science , vol.270 , Issue.5244 , pp. 2008-2011
    • Yamaguchi, K.1    Shirakabe, K.2    Shibuya, H.3    Irie, K.4    Oishi, I.5    Ueno, N.6    Taniguchi, T.7    Nishida, E.8    Matsumoto, K.9
  • 10
    • 0034595826 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1
    • DOI 10.1016/S0014-5793(00)01588-X, PII S001457930001588X
    • Sakurai, H., Miyoshi, H., Mizukami, J., and Sugita, T. (2000) Phosphorylation- dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1. FEBS Lett. 474, 141-145 (Pubitemid 30330823)
    • (2000) FEBS Letters , vol.474 , Issue.2-3 , pp. 141-145
    • Sakurai, H.1    Miyoshi, H.2    Mizukami, J.3    Sugita, T.4
  • 11
    • 0035968214 scopus 로고    scopus 로고
    • An evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKK
    • Ono, K., Ohtomo, T., Sato, S., Sugamata, Y., Suzuki, M., Hisamoto, N., Ninomiya-Tsuji, J., Tsuchiya, M., and Matsumoto, K. (2001) An evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKK. J. Biol. Chem. 276, 24396-24400
    • (2001) J. Biol. Chem. , vol.276 , pp. 24396-24400
    • Ono, K.1    Ohtomo, T.2    Sato, S.3    Sugamata, Y.4    Suzuki, M.5    Hisamoto, N.6    Ninomiya-Tsuji, J.7    Tsuchiya, M.8    Matsumoto, K.9
  • 12
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu, G., Kishida, S., Hiyama, A., Yamaguchi, K., Shibuya, H., Irie, K., Ninomiya-Tsuji, J., and Matsumoto, K. (2000) TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol. Cell 5, 649-658
    • (2000) Mol. Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6    Ninomiya-Tsuji, J.7    Matsumoto, K.8
  • 13
    • 0036788753 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol
    • Jiang, Z., Ninomiya-Tsuji, J., Qian, Y., Matsumoto, K., and Li, X. (2002) Interleukin-1 (IL-1) receptor-associated kinase-dependent IL-1-induced signaling complexes phosphorylate TAK1 and TAB2 at the plasma membrane and activate TAK1 in the cytosol. Mol. Cell. Biol. 22, 7158-7167
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7158-7167
    • Jiang, Z.1    Ninomiya-Tsuji, J.2    Qian, Y.3    Matsumoto, K.4    Li, X.5
  • 14
    • 1542314841 scopus 로고    scopus 로고
    • TAB3, a new binding partner of the protein kinase TAK1
    • DOI 10.1042/BJ20031794
    • Cheung, P. C., Nebreda, A. R., and Cohen, P. (2004) TAB3, a new binding partner of the protein kinase TAK1. Biochem. J. 378, 27-34 (Pubitemid 38299541)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 27-34
    • Cheung, P.C.F.1    Nebreda, A.R.2    Cohen, P.3
  • 15
    • 0034629146 scopus 로고    scopus 로고
    • TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop
    • DOI 10.1074/jbc.275.10.7359
    • Kishimoto, K., Matsumoto, K., and Ninomiya-Tsuji, J. (2000) TAK1 mitogen- activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop. J. Biol. Chem. 275, 7359-7364 (Pubitemid 30146289)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.10 , pp. 7359-7364
    • Kishimoto, K.1    Matsumoto, K.2    Ninomiya-Tsuji, J.3
  • 16
    • 14844295421 scopus 로고    scopus 로고
    • Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-β-activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding protein TAB1 and TAB2
    • DOI 10.1074/jbc.M407537200
    • Singhirunnusorn, P., Suzuki, S., Kawasaki, N., Saiki, I., and Sakurai, H. (2005) Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-β- activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding proteins TAB1 and TAB2. J. Biol. Chem. 280, 7359-7368 (Pubitemid 40341294)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 7359-7368
    • Singhirunnusorn, P.1    Suzuki, S.2    Kawasaki, N.3    Saiki, I.4    Sakurai, H.5
  • 17
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • DOI 10.1146/annurev.immunol.18.1.621
    • Karin, M., and Ben-Neriah, Y. (2000) Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621-663 (Pubitemid 30365393)
    • (2000) Annual Review of Immunology , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 18
    • 0028170265 scopus 로고
    • Activation of NF-κB in vivo is regulated by multiple phosphorylations
    • Naumann, M., and Scheidereit, C. (1994) Activation of NF-κB in vivo is regulated by multiple phosphorylations. EMBO J. 13, 4597-4607
    • (1994) EMBO J. , vol.13 , pp. 4597-4607
    • Naumann, M.1    Scheidereit, C.2
  • 19
    • 62149114138 scopus 로고    scopus 로고
    • Dual-specificity phosphatases: Critical regulators with diverse cellular targets
    • Patterson, K. I., Brummer, T., O'Brien, P. M., and Daly, R. J. (2009) Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem. J. 418, 475-489
    • (2009) Biochem. J. , vol.418 , pp. 475-489
    • Patterson, K.I.1    Brummer, T.2    O'Brien, P.M.3    Daly, R.J.4
  • 20
    • 70349582984 scopus 로고    scopus 로고
    • Overproduction, purification and structure determination of human dualspecificity phosphatase 14
    • Lountos, G. T., Tropea, J. E., Cherry, S., and Waugh, D. S. (2009) Overproduction, purification and structure determination of human dualspecificity phosphatase 14. Acta Crystallogr. D Biol. Crystallogr. 65, 1013-1020
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1013-1020
    • Lountos, G.T.1    Tropea, J.E.2    Cherry, S.3    Waugh, D.S.4
  • 21
    • 82755190610 scopus 로고    scopus 로고
    • Tripartite motif 8 (TRIM8) modulates TNFα- and IL-1β-triggered NF-κB activation by targeting TAK1 for K63-linked polyubiquitination
    • Li, Q., Yan, J., Mao, A. P., Li, C., Ran, Y., Shu, H.-B., and Wang, Y. Y. (2011) Tripartite motif 8 (TRIM8) modulates TNFα- and IL-1β-triggered NF-κB activation by targeting TAK1 for K63-linked polyubiquitination. Proc. Natl. Acad. Sci. U.S.A. 108, 19341-19346
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19341-19346
    • Li, Q.1    Yan, J.2    Mao, A.P.3    Li, C.4    Ran, Y.5    Shu, H.-B.6    Wang, Y.Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.