메뉴 건너뛰기




Volumn 32, Issue 23, 2012, Pages 4756-4768

IκB kinase ε phosphorylates TRAF2 to promote mammary epithelial cell transformation

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B KINASE EPSILON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYSINE; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2;

EID: 84871902988     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00468-12     Document Type: Article
Times cited : (56)

References (35)
  • 1
    • 11144289688 scopus 로고    scopus 로고
    • The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO
    • Abbott DW, Wilkins A, Asara JM, Cantley LC. 2004. The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO. Curr. Biol. 14:2217-2227.
    • (2004) Curr Biol , vol.14 , pp. 2217-2227
    • Abbott, D.W.1    Wilkins, A.2    Asara, J.M.3    Cantley, L.C.4
  • 2
    • 84934436838 scopus 로고    scopus 로고
    • Physiological roles and mechanisms of signaling by TRAF2 and TRAF5
    • Au PY, Yeh WC. 2007. Physiological roles and mechanisms of signaling by TRAF2 and TRAF5. Adv. Exp. Med. Biol. 597:32- 47.
    • (2007) Adv Exp Med Biol , vol.597
    • Au, P.Y.1    Yeh, W.C.2
  • 3
    • 58249115041 scopus 로고    scopus 로고
    • TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced gene expression and cell resistance to apoptosis
    • Blackwell K, et al. 2009. TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced gene expression and cell resistance to apoptosis. Mol. Cell. Biol. 29:303-314.
    • (2009) Mol Cell Biol , vol.29 , pp. 303-314
    • Blackwell, K.1
  • 4
    • 34249993765 scopus 로고    scopus 로고
    • Integrative genomic approaches identify IKBKE as a breast cancer oncogene
    • Boehm JS, et al. 2007. Integrative genomic approaches identify IKBKE as a breast cancer oncogene. Cell 129:1065-1079.
    • (2007) Cell , vol.129 , pp. 1065-1079
    • Boehm, J.S.1
  • 5
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp TR, Nijman SM, Dirac AM, Bernards R. 2003. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424:797- 801.
    • (2003) Nature , vol.424
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 6
    • 41549165085 scopus 로고    scopus 로고
    • Are the IKKs and IKK-related kinases TBK1 and IKK-epsilon similarly activated?
    • Chau TL, et al. 2008. Are the IKKs and IKK-related kinases TBK1 and IKK-epsilon similarly activated? Trends Biochem. Sci. 33:171-180.
    • (2008) Trends Biochem Sci , vol.33 , pp. 171-180
    • Chau, T.L.1
  • 7
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ. 2005. Ubiquitin signalling in the NF-kappaB pathway. Nat. Cell Biol. 7:758 -765.
    • (2005) Nat Cell Biol , vol.7
    • Chen, Z.J.1
  • 8
    • 66649127621 scopus 로고    scopus 로고
    • Mutations of multiple genes cause deregulation of NF-kappaB in diffuse large B-cell lymphoma
    • Compagno M, et al. 2009. Mutations of multiple genes cause deregulation of NF-kappaB in diffuse large B-cell lymphoma. Nature 459:717-721.
    • (2009) Nature , vol.459 , pp. 717-721
    • Compagno, M.1
  • 9
    • 0038393016 scopus 로고    scopus 로고
    • IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway
    • Fitzgerald KA, et al. 2003. IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. Nat. Immunol. 4:491- 496.
    • (2003) Nat Immunol , vol.4
    • Fitzgerald, K.A.1
  • 10
    • 54949147176 scopus 로고    scopus 로고
    • New regulators of NF-kappaB in inflammation
    • Ghosh S, Hayden MS. 2008. New regulators of NF-kappaB in inflammation. Nat. Rev. Immunol. 8:837- 848.
    • (2008) Nat Rev Immunol , vol.8
    • Ghosh, S.1    Hayden, M.S.2
  • 11
    • 4043088499 scopus 로고    scopus 로고
    • IKKbeta links inflammation and tumorigenesis in a mouse model of colitis-associated cancer
    • Greten FR, et al. 2004. IKKbeta links inflammation and tumorigenesis in a mouse model of colitis-associated cancer. Cell 118:285-296.
    • (2004) Cell , vol.118 , pp. 285-296
    • Greten, F.R.1
  • 12
    • 77954930632 scopus 로고    scopus 로고
    • IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer
    • Gyrd-Hansen M, Meier P. 2010. IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer. Nat. Rev. Cancer 10: 561-574.
    • (2010) Nat Rev Cancer , vol.10 , pp. 561-574
    • Gyrd-hansen, M.1    Meier, P.2
  • 13
    • 1542380581 scopus 로고    scopus 로고
    • Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB
    • Habelhah H, et al. 2004. Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB. EMBO J. 23:322-332.
    • (2004) EMBO J , vol.23 , pp. 322-332
    • Habelhah, H.1
  • 14
    • 17644391197 scopus 로고    scopus 로고
    • A rapid method for determining protein kinase phosphorylation specificity
    • Hutti JE, et al. 2004. A rapid method for determining protein kinase phosphorylation specificity. Nat. Methods 1:27-29.
    • (2004) Nat Methods , vol.1 , pp. 27-29
    • Hutti, J.E.1
  • 15
    • 65649114699 scopus 로고    scopus 로고
    • Phosphorylation of the tumor suppressor CYLD by the breast cancer oncogene IKKepsilon promotes cell transformation
    • Hutti JE, et al. 2009. Phosphorylation of the tumor suppressor CYLD by the breast cancer oncogene IKKepsilon promotes cell transformation. Mol. Cell 34:461- 472.
    • (2009) Mol Cell , vol.34
    • Hutti, J.E.1
  • 16
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-kappaB in cancer development and progression
    • Karin M. 2006. Nuclear factor-kappaB in cancer development and progression. Nature 441:431- 436.
    • (2006) Nature , vol.441
    • Karin, M.1
  • 17
    • 25844459154 scopus 로고    scopus 로고
    • NF-kappaB: linking inflammation and immunity to cancer development and progression
    • Karin M, Greten FR. 2005. NF-kappaB: linking inflammation and immunity to cancer development and progression. Nat. Rev. Immunol. 5:749 -759.
    • (2005) Nat Rev Immunol , vol.5
    • Karin, M.1    Greten, F.R.2
  • 18
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A, et al. 2003. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 424:801- 805.
    • (2003) Nature , vol.424
    • Kovalenko, A.1
  • 19
    • 17644383370 scopus 로고    scopus 로고
    • A pervasive role of ubiquitin conjugation in activation and termination of IkappaB kinase pathways
    • Krappmann D, Scheidereit C. 2005. A pervasive role of ubiquitin conjugation in activation and termination of IkappaB kinase pathways. EMBO Rep. 6:321-326.
    • (2005) EMBO Rep , vol.6 , pp. 321-326
    • Krappmann, D.1    Scheidereit, C.2
  • 20
    • 41149136296 scopus 로고    scopus 로고
    • Oncogenic CARD11 mutations in human diffuse large B cell lymphoma
    • Lenz G, et al. 2008. Oncogenic CARD11 mutations in human diffuse large B cell lymphoma. Science 319:1676 -1679.
    • (2008) Science , vol.319
    • Lenz, G.1
  • 21
    • 58149301485 scopus 로고    scopus 로고
    • PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination
    • Li S, Wang L, Dorf ME. 2009. PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination. Mol. Cell 33:30-42.
    • (2009) Mol Cell , vol.33 , pp. 30-42
    • Li, S.1    Wang, L.2    Dorf, M.E.3
  • 22
    • 70449109147 scopus 로고    scopus 로고
    • Requirement for NF-kappaB signalling in a mouse model of lung adenocarcinoma
    • Meylan E, et al. 2009. Requirement for NF-kappaB signalling in a mouse model of lung adenocarcinoma. Nature 462:104 -107.
    • (2009) Nature , vol.462
    • Meylan, E.1
  • 23
    • 66549086135 scopus 로고    scopus 로고
    • The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas
    • Novak U, et al. 2009. The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas. Blood 113:4918-4921.
    • (2009) Blood , vol.113 , pp. 4918-4921
    • Novak, U.1
  • 24
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • Perkins ND. 2007. Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat. Rev. Mol. Cell Biol. 8:49-62.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 25
    • 4644324186 scopus 로고    scopus 로고
    • NF-kappaB functions as a tumour promoter in inflammation-associated cancer
    • Pikarsky E, et al. 2004. NF-kappaB functions as a tumour promoter in inflammation-associated cancer. Nature 431:461- 466.
    • (2004) Nature , vol.431
    • Pikarsky, E.1
  • 26
    • 0033485542 scopus 로고    scopus 로고
    • NF-kappaB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase
    • Pomerantz JL, Baltimore D. 1999. NF-kappaB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase. EMBO J. 18:6694-6704.
    • (1999) EMBO J , vol.18 , pp. 6694-6704
    • Pomerantz, J.L.1    Baltimore, D.2
  • 27
    • 18144368948 scopus 로고    scopus 로고
    • Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation
    • Reiley W, Zhang M, Wu X, Granger E, Sun SC. 2005. Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation. Mol. Cell. Biol. 25:3886 -3895.
    • (2005) Mol Cell Biol , vol.25
    • Reiley, W.1    Zhang, M.2    Wu, X.3    Granger, E.4    Sun, S.C.5
  • 28
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-kappa B by TNF receptor 2 and CD40
    • Rothe M, Sarma V, Dixit VM, Goeddel DV. 1995. TRAF2-mediated activation of NF-kappa B by TNF receptor 2 and CD40. Science 269:1424- 1427.
    • (1995) Science , vol.269
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 29
    • 0038150358 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor- associated factor 2 (TRAF2)
    • Shi CS, Kehrl JH. 2003. Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor- associated factor 2 (TRAF2). J. Biol. Chem. 278:15429 -15434.
    • (2003) J Biol Chem , vol.278
    • Shi, C.S.1    Kehrl, J.H.2
  • 30
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun SC. 2008. Deubiquitylation and regulation of the immune response. Nat. Rev. Immunol. 8:501-511.
    • (2008) Nat Rev Immunol , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 31
    • 65949114424 scopus 로고    scopus 로고
    • Phosphorylation of TRAF2 within its RING domain inhibits stress-induced cell death by promoting IKK and suppressing JNK activation
    • Thomas GS, Zhang L, Blackwell K, Habelhah H. 2009. Phosphorylation of TRAF2 within its RING domain inhibits stress-induced cell death by promoting IKK and suppressing JNK activation. Cancer Res. 69:3665- 3672.
    • (2009) Cancer Res , vol.69
    • Thomas, G.S.1    Zhang, L.2    Blackwell, K.3    Habelhah, H.4
  • 32
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E, et al. 2003. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424:793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1
  • 33
    • 72149117664 scopus 로고    scopus 로고
    • TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-{kappa}B and to prevent TNF-induced apoptosis
    • Vince JE, et al. 2009. TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-{kappa}B and to prevent TNF-induced apoptosis. J. Biol. Chem. 284:35906 -35915.
    • (2009) J Biol Chem , vol.284
    • Vince, J.E.1
  • 34
    • 20044387665 scopus 로고    scopus 로고
    • TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination
    • Wu CJ, et al. 2005. TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination. EMBO J. 24:1886 -1898.
    • (2005) EMBO J , vol.24
    • Wu, C.J.1
  • 35
    • 78651084030 scopus 로고    scopus 로고
    • TRAF2 phosphorylation promotes NF-{kappa}B-dependent gene expression and inhibits oxidative stress-induced cell death
    • Zhang L, Blackwell K, Altaeva A, Shi Z, Habelhah H. 2011. TRAF2 phosphorylation promotes NF-{kappa}B-dependent gene expression and inhibits oxidative stress-induced cell death. Mol. Biol. Cell 22: 128 -140.
    • (2011) Mol Biol Cell , vol.22
    • Zhang, L.1    Blackwell, K.2    Altaeva, A.3    Shi, Z.4    Habelhah, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.