메뉴 건너뛰기




Volumn 129, Issue 7, 2016, Pages 1455-1467

TRAF2 exerts opposing effects on basal and TNFα-induced activation of the classic IKK complex in hematopoietic cells in mice

Author keywords

Apoptosis; NF B; TNF ; TRAF2; TRAF5

Indexed keywords

CASPASE 8; I KAPPA B KINASE; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 5; BIRC2 PROTEIN, MOUSE; BIRC3 PROTEIN, MOUSE; CCL5 PROTEIN, MOUSE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INDUCIBLE NITRIC OXIDE SYNTHASE; INHIBITOR OF APOPTOSIS PROTEIN; NOS2 PROTEIN, MOUSE; RANTES; TUMOR NECROSIS FACTOR; UBIQUITIN PROTEIN LIGASE;

EID: 84964045814     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.180554     Document Type: Article
Times cited : (9)

References (41)
  • 2
    • 84878376898 scopus 로고    scopus 로고
    • Two coordinated mechanisms underlie tumor necrosis factor alpha-induced immediate and delayed IkappaB kinase activation
    • Blackwell, K., Zhang, L., Workman, L. M., Ting, A. T., Iwai, K. and Habelhah, H. (2013). Two coordinated mechanisms underlie tumor necrosis factor alpha-induced immediate and delayed IkappaB kinase activation. Mol. Cell. Biol. 33, 1901-1915.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 1901-1915
    • Blackwell, K.1    Zhang, L.2    Workman, L.M.3    Ting, A.T.4    Iwai, K.5    Habelhah, H.6
  • 3
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • Bonizzi, G. and Karin, M. (2004). The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 25, 280-288.
    • (2004) Trends Immunol. , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 4
    • 0035475338 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factors (TRAFs)
    • Bradley, J. R. and Pober, J. S. (2001). Tumor necrosis factor receptor-associated factors (TRAFs). Oncogene 20, 6482-6491.
    • (2001) Oncogene , vol.20 , pp. 6482-6491
    • Bradley, J.R.1    Pober, J.S.2
  • 5
    • 33344476184 scopus 로고    scopus 로고
    • cFLIP regulation of lymphocyte activation and development
    • Budd, R. C., Yeh, W.-C. and Tschopp, J. (2006). cFLIP regulation of lymphocyte activation and development. Nat. Rev. Immunol. 6, 196-204.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 196-204
    • Budd, R.C.1    Yeh, W.-C.2    Tschopp, J.3
  • 6
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen, Z. J. and Sun, L. J. (2009). Nonproteolytic functions of ubiquitin in cell signaling. Mol. Cell 33, 275-286.
    • (2009) Mol. Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 7
    • 68949086679 scopus 로고    scopus 로고
    • Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2
    • Csomos, R. A., Brady, G. F. and Duckett, C. S. (2009). Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2. J. Biol. Chem. 284, 20531-20539.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20531-20539
    • Csomos, R.A.1    Brady, G.F.2    Duckett, C.S.3
  • 8
    • 77952912228 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding
    • Feltham, R., Moulin, M., Vince, J. E., Mace, P. D., Wong, W. W. L., Anderton, H., Day, C. L., Vaux, D. L. and Silke, J. (2010). Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding. J. Biol. Chem. 285, 17525-17536.
    • (2010) J. Biol. Chem. , vol.285 , pp. 17525-17536
    • Feltham, R.1    Moulin, M.2    Vince, J.E.3    Mace, P.D.4    Wong, W.W.L.5    Anderton, H.6    Day, C.L.7    Vaux, D.L.8    Silke, J.9
  • 9
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas, T. L., Emmerich, C. H., Gerlach, B., Schmukle, A. C., Cordier, S. M., Rieser, E., Feltham, R., Vince, J., Warnken, U., Wenger, T. et al. (2009). Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 36, 831-844.
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6    Feltham, R.7    Vince, J.8    Warnken, U.9    Wenger, T.10
  • 10
    • 79952831701 scopus 로고    scopus 로고
    • Emerging complexity of protein ubiquitination in the NF-kappaB pathway
    • Habelhah, H. (2010). Emerging complexity of protein ubiquitination in the NF-kappaB pathway. Genes Cancer 1, 735-747.
    • (2010) Genes Cancer , vol.1 , pp. 735-747
    • Habelhah, H.1
  • 11
    • 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., Takahashi, S., Cho, S.-G., Kadoya, T., Watanabe, T. and Ronai, Z. (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    Takahashi, S.2    Cho, S.-G.3    Kadoya, T.4    Watanabe, T.5    Ronai, Z.6
  • 12
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden, M. S. and Ghosh, S. (2008). Shared principles in NF-kappaB signaling. Cell 132, 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 14
    • 0037044575 scopus 로고    scopus 로고
    • The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation
    • Hoffmann, A., Levchenko, A., Scott, M. L. and Baltimore, D. (2002). The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation. Science 298, 1241-1245.
    • (2002) Science , vol.298 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 15
    • 0142105387 scopus 로고    scopus 로고
    • Genetic analysis of NF-kappaB/Rel transcription factors defines functional specificities
    • Hoffmann, A., Leung, T. H. and Baltimore, D. (2003). Genetic analysis of NF-kappaB/Rel transcription factors defines functional specificities. EMBO J. 22, 5530-5539.
    • (2003) EMBO J. , vol.22 , pp. 5530-5539
    • Hoffmann, A.1    Leung, T.H.2    Baltimore, D.3
  • 16
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: a new regulator of NF-kappaB activation
    • Iwai, K. and Tokunaga, F. (2009). Linear polyubiquitination: a new regulator of NF-kappaB activation. EMBO Rep. 10, 706-713.
    • (2009) EMBO Rep. , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 17
    • 71849094168 scopus 로고    scopus 로고
    • TNF receptor-associated factor 5 is required for optimal T cell expansion and survival in response to infection
    • Kraus, Z. J., Haring, J. S. and Bishop, G. A. (2008). TNF receptor-associated factor 5 is required for optimal T cell expansion and survival in response to infection. J. Immunol. 181, 7800-7809.
    • (2008) J. Immunol. , vol.181 , pp. 7800-7809
    • Kraus, Z.J.1    Haring, J.S.2    Bishop, G.A.3
  • 18
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • Lee, T. H., Shank, J., Cusson, N. and Kelliher, M. A. (2004). The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J. Biol. Chem. 279, 33185-33191.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 19
    • 81055145273 scopus 로고    scopus 로고
    • Crucial role for TNF receptor-associated factor 2 (TRAF2) in regulating NF-kappaB2 signaling that contributes to autoimmunity
    • Lin, W.-J., Su, Y.-W., Lu, Y.-C., Hao, Z., Chio, I. I., Chen, N.-J., Brustle, A., Li, W. Y. and Mak, T.W. (2011). Crucial role for TNF receptor-associated factor 2 (TRAF2) in regulating NF-kappaB2 signaling that contributes to autoimmunity. Proc. Natl. Acad. Sci. USA 108, 18354-18359.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18354-18359
    • Lin, W.-J.1    Su, Y.-W.2    Lu, Y.-C.3    Hao, Z.4    Chio, I.I.5    Chen, N.-J.6    Brustle, A.7    Li, W.Y.8    Mak, T.W.9
  • 27
    • 0037384905 scopus 로고    scopus 로고
    • c-Jun NH(2)-terminal kinase is essential for the regulation of AP-1 by tumor necrosis factor
    • Ventura, J.-J., Kennedy, N. J., Lamb, J. A., Flavell, R. A. and Davis, R. J. (2003). c-Jun NH(2)-terminal kinase is essential for the regulation of AP-1 by tumor necrosis factor. Mol. Cell. Biol. 23, 2871-2882.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 2871-2882
    • Ventura, J.-J.1    Kennedy, N.J.2    Lamb, J.A.3    Flavell, R.A.4    Davis, R.J.5
  • 29
    • 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, J. E., Pantaki, D., Feltham, R., Mace, P. D., Cordier, S. M., Schmukle, A. C., Davidson, A. J., Callus, B. A., Wong, W. W., Gentle, I. E. 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 , pp. 35906-35915
    • Vince, J.E.1    Pantaki, D.2    Feltham, R.3    Mace, P.D.4    Cordier, S.M.5    Schmukle, A.C.6    Davidson, A.J.7    Callus, B.A.8    Wong, W.W.9    Gentle, I.E.10
  • 30
    • 79952498248 scopus 로고    scopus 로고
    • TNFR1-induced activation of the classical NF-kappaB pathway
    • Wajant, H. and Scheurich, P. (2011). TNFR1-induced activation of the classical NF-kappaB pathway. FEBS J. 278, 862-876.
    • (2011) FEBS J. , vol.278 , pp. 862-876
    • Wajant, H.1    Scheurich, P.2
  • 31
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang, C. Y., Mayo, M. W., Korneluk, R. G., Goeddel, D. V. and Baldwin, A. S., Jr (1998). NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281, 1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin, A.S.5
  • 32
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang, L., Du, F. and Wang, X. (2008). TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133, 693-703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 34
    • 84878350055 scopus 로고    scopus 로고
    • TNFR1 signaling kinetics: spatiotemporal control of three phases of IKK activation by posttranslational modification
    • Workman, L. M. and Habelhah, H. (2013). TNFR1 signaling kinetics: spatiotemporal control of three phases of IKK activation by posttranslational modification. Cell Signal. 25, 1654-1664.
    • (2013) Cell Signal. , vol.25 , pp. 1654-1664
    • Workman, L.M.1    Habelhah, H.2
  • 35
    • 33645703930 scopus 로고    scopus 로고
    • NEMO is a sensor of Lys 63-linked polyubiquitination and functions in NF-κB activation
    • Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. and Ashwell, J. D. (2006). NEMO is a sensor of Lys 63-linked polyubiquitination and functions in NF-κB activation. Nat. Cell Biol. 8, 398-406.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 38
    • 70449424269 scopus 로고    scopus 로고
    • Structural basis for the lack of E2 interaction in the RING domain of TRAF2
    • Yin, Q., Lamothe, B., Darnay, B. G. and Wu, H. (2009). Structural basis for the lack of E2 interaction in the RING domain of TRAF2. Biochemistry 48, 10558-10567.
    • (2009) Biochemistry , vol.48 , pp. 10558-10567
    • Yin, Q.1    Lamothe, B.2    Darnay, B.G.3    Wu, H.4
  • 39
    • 42149110830 scopus 로고    scopus 로고
    • Control of canonical NF-kappaB activation through the NIK-IKK complex pathway
    • Zarnegar, B., Yamazaki, S., He, J. Q. and Cheng, G. (2008). Control of canonical NF-kappaB activation through the NIK-IKK complex pathway. Proc. Natl. Acad. Sci. USA 105, 3503-3508.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3503-3508
    • Zarnegar, B.1    Yamazaki, S.2    He, J.Q.3    Cheng, G.4
  • 40
    • 65649150701 scopus 로고    scopus 로고
    • TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells
    • Zhang, L., Blackwell, K., Thomas, G. S., Sun, S., Yeh, W.-C. and Habelhah, H. (2009). TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells. J. Mol. Biol. 389, 495-510.
    • (2009) J. Mol. Biol. , vol.389 , pp. 495-510
    • Zhang, L.1    Blackwell, K.2    Thomas, G.S.3    Sun, S.4    Yeh, W.-C.5    Habelhah, H.6
  • 41
    • 77949332322 scopus 로고    scopus 로고
    • The RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB
    • Zhang, L., Blackwell, K., Shi, Z. and Habelhah, H. (2010). The RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB. J. Mol. Biol. 396, 528-539.
    • (2010) J. Mol. Biol. , vol.396 , pp. 528-539
    • Zhang, L.1    Blackwell, K.2    Shi, Z.3    Habelhah, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.