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Volumn 5, Issue 216, 2012, Pages

Cell biology: Cellular inhibitors of apoptosis are global regulators of NF-κB and MAPK activation by members of the TNF family of receptors

Author keywords

[No Author keywords available]

Indexed keywords

B CELL ACTIVATING FACTOR RECEPTOR; I KAPPA B; I KAPPA B KINASE BETA; I KAPPA B KINASE GAMMA; I KAPPA B KINASE INHIBITOR; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE 1; PROTEASOME; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; UBIQUITIN PROTEIN LIGASE E3; CARRIER PROTEIN; I KAPPA B KINASE; IKBKG PROTEIN, HUMAN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; INTERLEUKIN 4 RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; RNF31 PROTEIN, HUMAN; SMALL INTERFERING RNA; UBIQUITIN;

EID: 84858627919     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2001878     Document Type: Article
Times cited : (172)

References (60)
  • 2
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • R. M. Locksley, N. Killeen, M. J. Lenardo, The TNF and TNF receptor superfamilies: Integrating mammalian biology. Cell 104, 487-501 (2001).
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 4
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • H. Häcker, M. Karin, Regulation and function of IKK and IKK-related kinases. Sci. STKE 2006, re13 (2006).
    • (2006) Sci. STKE , vol.2006
    • Häcker, H.1    Karin, M.2
  • 5
    • 37449033866 scopus 로고    scopus 로고
    • Positive and negative signaling components involved in TNFα-induced NF-κB activation
    • H. Li, X. Lin, Positive and negative signaling components involved in TNFα-induced NF-κB activation. Cytokine 41, 1-8 (2008).
    • (2008) Cytokine , vol.41 , pp. 1-8
    • Li, H.1    Lin, X.2
  • 6
    • 67749117934 scopus 로고    scopus 로고
    • Signal integration by JNK and p38 MAPK pathways in cancer development
    • E. F. Wagner, A. R. Nebreda, Signal integration by JNK and p38 MAPK pathways in cancer development. Nat. Rev. Cancer 9, 537-549 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 537-549
    • Wagner, E.F.1    Nebreda, A.R.2
  • 7
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • V. Baud, M. Karin, Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 11, 372-377 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 8
    • 33750443289 scopus 로고    scopus 로고
    • IκB kinase complexes: Gateways to NF-κB activation and transcription
    • C. Scheidereit, IκB kinase complexes: Gateways to NF-κB activation and transcription. Oncogene 25, 6685-6705 (2006).
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 9
    • 33749265867 scopus 로고    scopus 로고
    • The alternative NF-κB pathway from biochemistry to biology: Pitfalls and promises for future drug development
    • E. Dejardin, The alternative NF-κB pathway from biochemistry to biology: Pitfalls and promises for future drug development. Biochem. Pharmacol. 72, 1161-1179 (2006).
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1161-1179
    • Dejardin, E.1
  • 10
    • 45849120966 scopus 로고    scopus 로고
    • (Un)expected roles of c-IAPs in apoptotic and NFκB signaling pathways
    • E. Varfolomeev, D. Vucic, (Un)expected roles of c-IAPs in apoptotic and NFκB signaling pathways. Cell Cycle 7, 1511-1521 (2008).
    • (2008) Cell Cycle , vol.7 , pp. 1511-1521
    • Varfolomeev, E.1    Vucic, D.2
  • 11
    • 77449147556 scopus 로고    scopus 로고
    • Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs
    • J. Silke, R. Brink, Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs. Cell Death Differ. 17, 35-45 (2010).
    • (2010) Cell Death Differ. , vol.17 , pp. 35-45
    • Silke, J.1    Brink, R.2
  • 12
    • 44749093460 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of TNFR1 signaling
    • I. E. Wertz, V. M. Dixit, Ubiquitin-mediated regulation of TNFR1 signaling. Cytokine Growth Factor Rev. 19, 313-324 (2008).
    • (2008) Cytokine Growth Factor Rev. , vol.19 , pp. 313-324
    • Wertz, I.E.1    Dixit, V.M.2
  • 15
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • O. Micheau, J. Tschopp, Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114, 181-190 (2003).
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 20
    • 0038708366 scopus 로고    scopus 로고
    • The Fn14 cytoplasmic tail binds tumour-necrosis-factor-receptor- associated factors 1, 2, 3 and 5 and mediates nuclear factor-κB activation
    • S. A. Brown, C. M. Richards, H. N. Hanscom, S. L. Feng, J. A. Winkles, The Fn14 cytoplasmic tail binds tumour-necrosis-factor-receptor-associated factors 1, 2, 3 and 5 and mediates nuclear factor-κB activation. Biochem. J. 371, 395-403 (2003).
    • (2003) Biochem. J. , vol.371 , pp. 395-403
    • Brown, S.A.1    Richards, C.M.2    Hanscom, H.N.3    Feng, S.L.4    Winkles, J.A.5
  • 21
    • 0036038231 scopus 로고    scopus 로고
    • Lymphotoxin b receptor induces interleukin 8 gene expression via NF-κB and AP-1 activation
    • Y. H. Chang, S. L. Hsieh, M. C. Chen, W. W. Lin, Lymphotoxin b receptor induces interleukin 8 gene expression via NF-κB and AP-1 activation. Exp. Cell Res. 278, 166-174 (2002).
    • (2002) Exp. Cell Res. , vol.278 , pp. 166-174
    • Chang, Y.H.1    Hsieh, S.L.2    Chen, M.C.3    Lin, W.W.4
  • 22
    • 14844343590 scopus 로고    scopus 로고
    • TRAF2 plays a key, nonredundant role in LIGHT-lymphotoxin β receptor signaling
    • Y. S. Kim, S. A. Nedospasov, Z. G. Liu, TRAF2 plays a key, nonredundant role in LIGHT-lymphotoxin β receptor signaling. Mol. Cell. Biol. 25, 2130-2137 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2130-2137
    • Kim, Y.S.1    Nedospasov, S.A.2    Liu, Z.G.3
  • 24
    • 0141531101 scopus 로고    scopus 로고
    • TL1A-induced NF-κB activation and c-IAP2 production prevent DR3-mediated apoptosis in TF-1 cells
    • L. Wen, L. Zhuang, X. Luo, P. Wei, TL1A-induced NF-κB activation and c-IAP2 production prevent DR3-mediated apoptosis in TF-1 cells. J. Biol. Chem. 278, 39251-39258 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 39251-39258
    • Wen, L.1    Zhuang, L.2    Luo, X.3    Wei, P.4
  • 25
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • M. Rothe, M. G. Pan, W. J. Henzel, T. M. Ayres, D. V. Goeddel, The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83, 1243-1252 (1995).
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 28
    • 0037149542 scopus 로고    scopus 로고
    • TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2
    • X. Li, Y. Yang, J. D. Ashwell, TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature 416, 345-347 (2002).
    • (2002) Nature , vol.416 , pp. 345-347
    • Li, X.1    Yang, Y.2    Ashwell, J.D.3
  • 31
    • 56349164232 scopus 로고    scopus 로고
    • Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling
    • S. Vallabhapurapu, A. Matsuzawa, W. Zhang, P. H. Tseng, J. J. Keats, H. Wang, D. A. Vignali, P. L. Bergsagel, M. Karin, Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling. Nat. Immunol. 9, 1364-1370 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 1364-1370
    • Vallabhapurapu, S.1    Matsuzawa, A.2    Zhang, W.3    Tseng, P.H.4    Keats, J.J.5    Wang, H.6    Vignali, D.A.7    Bergsagel, P.L.8    Karin, M.9
  • 37
    • 0036794398 scopus 로고    scopus 로고
    • BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells
    • E. Claudio, K. Brown, S. Park, H. Wang, U. Siebenlist, BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells. Nat. Immunol. 3, 958-965 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 958-965
    • Claudio, E.1    Brown, K.2    Park, S.3    Wang, H.4    Siebenlist, U.5
  • 39
    • 0037114130 scopus 로고    scopus 로고
    • TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NF-κB activation and IL-10 production
    • L. G. Xu, H. B. Shu, TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NF-κB activation and IL-10 production. J. Immunol. 169, 6883-6889 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 6883-6889
    • Xu, L.G.1    Shu, H.B.2
  • 40
    • 10344226678 scopus 로고    scopus 로고
    • Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: Implications for intracellular signaling regulation
    • C. Z. Ni, G. Oganesyan, K. Welsh, X. Zhu, J. C. Reed, A. C. Satterthwait, G. Cheng, K. R. Ely, Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: Implications for intracellular signaling regulation. J. Immunol. 173, 7394-7400 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 7394-7400
    • Ni, C.Z.1    Oganesyan, G.2    Welsh, K.3    Zhu, X.4    Reed, J.C.5    Satterthwait, A.C.6    Cheng, G.7    Ely, K.R.8
  • 44
    • 70449424269 scopus 로고    scopus 로고
    • Structural basis for the lack of E2 interaction in the RING domain of TRAF2
    • Q. Yin, B. Lamothe, B. G. Darnay, H. Wu, Structural basis for the lack of E2 interaction in the RING domain of TRAF2. Biochemistry 48, 10558-10567 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10558-10567
    • Yin, Q.1    Lamothe, B.2    Darnay, B.G.3    Wu, H.4
  • 47
    • 33646502116 scopus 로고    scopus 로고
    • If the prophet does not come to the mountain: Dynamics of signaling complexes in NF-κB activation
    • A. Kovalenko, D. Wallach, If the prophet does not come to the mountain: Dynamics of signaling complexes in NF-κB activation. Mol. Cell 22, 433-436 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 433-436
    • Kovalenko, A.1    Wallach, D.2
  • 49
    • 0037037545 scopus 로고    scopus 로고
    • Regulation of the subcellular localization of tumor necrosis factor receptor-associated factor (TRAF)2 by TRAF1 reveals mechanisms of TRAF2 signaling
    • J. R. Arron, Y. Pewzner-Jung, M. C. Walsh, T. Kobayashi, Y. Choi, Regulation of the subcellular localization of tumor necrosis factor receptor-associated factor (TRAF)2 by TRAF1 reveals mechanisms of TRAF2 signaling. J. Exp. Med. 196, 923-934 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 923-934
    • Arron, J.R.1    Pewzner-Jung, Y.2    Walsh, M.C.3    Kobayashi, T.4    Choi, Y.5
  • 50
    • 0037205442 scopus 로고    scopus 로고
    • Regulation of TRAF2 signaling by self-induced degradation
    • K. D. Brown, B. S. Hostager, G. A. Bishop, Regulation of TRAF2 signaling by self-induced degradation. J. Biol. Chem. 277, 19433-19438 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 19433-19438
    • Brown, K.D.1    Hostager, B.S.2    Bishop, G.A.3
  • 51
    • 20044387665 scopus 로고    scopus 로고
    • TNF-α induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination
    • C. J. Wu, D. B. Conze, X. Li, S. X. Ying, J. A. Hanover, J. D. Ashwell, TNF-α induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination. EMBO J. 24, 1886-1898 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1886-1898
    • Wu, C.J.1    Conze, D.B.2    Li, X.3    Ying, S.X.4    Hanover, J.A.5    Ashwell, J.D.6
  • 52
    • 33544470185 scopus 로고    scopus 로고
    • TRAF2: A double-edged sword?
    • Z. P. Xia, Z. J. Chen, TRAF2: A double-edged sword? Sci. STKE 2005, pe7 (2005).
    • (2005) Sci. STKE , vol.2005
    • Xia, Z.P.1    Chen, Z.J.2
  • 54
    • 77950352082 scopus 로고    scopus 로고
    • Crystal structures of the TRAF2: CIAP2 and the TRAF1: TRAF2: cIAP2 complexes: Affinity, specificity, and regulation
    • C. Zheng, V. Kabaleeswaran, Y. Wang, G. Cheng, H. Wu, Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: Affinity, specificity, and regulation. Mol. Cell 38, 101-113 (2010).
    • (2010) Mol. Cell , vol.38 , pp. 101-113
    • Zheng, C.1    Kabaleeswaran, V.2    Wang, Y.3    Cheng, G.4    Wu, H.5
  • 55
    • 57649120782 scopus 로고    scopus 로고
    • Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment
    • P. D. Mace, K. Linke, R. Feltham, F. R. Schumacher, C. A. Smith, D. L. Vaux, J. Silke, C. L. Day, Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment. J. Biol. Chem. 283, 31633-31640 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31633-31640
    • Mace, P.D.1    Linke, K.2    Feltham, R.3    Schumacher, F.R.4    Smith, C.A.5    Vaux, D.L.6    Silke, J.7    Day, C.L.8
  • 56
    • 77949485585 scopus 로고    scopus 로고
    • Targeting inhibitor of apoptosis proteins for therapeutic intervention
    • C. Ndubaku, F. Cohen, E. Varfolomeev, D. Vucic, Targeting inhibitor of apoptosis proteins for therapeutic intervention. Future Med. Chem. 1, 1509-1525 (2009).
    • (2009) Future Med. Chem. , vol.1 , pp. 1509-1525
    • Ndubaku, C.1    Cohen, F.2    Varfolomeev, E.3    Vucic, D.4
  • 60
    • 0037332043 scopus 로고    scopus 로고
    • Loss of TACI causes fatal lymphoproliferation and autoimmunity, establishing TACI as an inhibitory BLyS receptor
    • D. Seshasayee, P. Valdez, M. Yan, V. M. Dixit, D. Tumas, I. S. Grewal, Loss of TACI causes fatal lymphoproliferation and autoimmunity, establishing TACI as an inhibitory BLyS receptor. Immunity 18, 279-288 (2003).
    • (2003) Immunity , vol.18 , pp. 279-288
    • Seshasayee, D.1    Valdez, P.2    Yan, M.3    Dixit, V.M.4    Tumas, D.5    Grewal, I.S.6


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