메뉴 건너뛰기




Volumn 457, Issue 7231, 2009, Pages 906-909

ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development

Author keywords

[No Author keywords available]

Indexed keywords

ABIN 1 PROTEIN; CASPASE 8; FAS ASSOCIATED DEATH DOMAIN PROTEIN; POLYUBIQUITIN; PROTEIN INHIBITOR; TUMOR NECROSIS FACTOR; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 60149104060     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07575     Document Type: Article
Times cited : (139)

References (24)
  • 1
    • 0033612571 scopus 로고    scopus 로고
    • The zinc finger protein A20 inhibits TNF-induced NF-κB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-κB-inhibiting protein ABIN-1
    • Heyninck, K. et al. The zinc finger protein A20 inhibits TNF-induced NF-κB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-κB-inhibiting protein ABIN-1. J. Cell Biol. 145, 1471-1482 (1999).
    • (1999) J. Cell Biol , vol.145 , pp. 1471-1482
    • Heyninck, K.1
  • 2
    • 0025179989 scopus 로고
    • The A20 cDNA induced by tumor necrosis factor α encodes a novel type of zinc finger protein
    • Opipari, A. W. Jr, Boguski, M. S. & Dixit, V. M. The A20 cDNA induced by tumor necrosis factor α encodes a novel type of zinc finger protein. J. Biol. Chem. 265, 14705-14708 (1990).
    • (1990) J. Biol. Chem , vol.265 , pp. 14705-14708
    • Opipari Jr, A.W.1    Boguski, M.S.2    Dixit, V.M.3
  • 3
    • 0032980504 scopus 로고    scopus 로고
    • Absence of tumor necrosis factor rescues RelA-deficient mice from embryonic lethality
    • Doi, T. S. et al. Absence of tumor necrosis factor rescues RelA-deficient mice from embryonic lethality. Proc. Natl Acad. Sci. USA 96, 2994-2999 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2994-2999
    • Doi, T.S.1
  • 4
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • Beg, A. A. & Baltimore, D. An essential role for NF-κB in preventing TNF-α-induced cell death. Science 274, 782-784 (1996).
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 5
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB
    • Wang, C. Y., Mayo, M. W. & Baldwin, A. S. Jr. TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB. Science 274, 784-787 (1996).
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin Jr., A.S.3
  • 7
    • 23044478028 scopus 로고    scopus 로고
    • Adenoviral gene transfer of ABIN-1 protects mice from TNF/galactosamine-induced acute liver failure and lethality
    • Wullaert, A. et al. Adenoviral gene transfer of ABIN-1 protects mice from TNF/galactosamine-induced acute liver failure and lethality. Hepatology 42, 381-389 (2005).
    • (2005) Hepatology , vol.42 , pp. 381-389
    • Wullaert, A.1
  • 9
    • 0035889252 scopus 로고    scopus 로고
    • Induction of gadd45β by NF-κB downregulates pro-apoptotic JNK signalling
    • De Smaele, E. et al. Induction of gadd45β by NF-κB downregulates pro-apoptotic JNK signalling. Nature 414, 308-313 (2001).
    • (2001) Nature , vol.414 , pp. 308-313
    • De Smaele, E.1
  • 10
    • 0035891320 scopus 로고    scopus 로고
    • Inhibition of JNK activation through NF-κB target genes
    • Tang, G. et al. Inhibition of JNK activation through NF-κB target genes. Nature 414, 313-317 (2001).
    • (2001) Nature , vol.414 , pp. 313-317
    • Tang, G.1
  • 11
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFα-induced cell death by inducing c-FLIP(L) turnover
    • Chang, L. et al. The E3 ubiquitin ligase itch couples JNK activation to TNFα-induced cell death by inducing c-FLIP(L) turnover. Cell 124, 601-613 (2006).
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1
  • 12
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NF-κB and cell death responses in A20-deficient mice
    • Lee, E. G. et al. Failure to regulate TNF-induced NF-κB and cell death responses in A20-deficient mice. Science 289, 2350-2354 (2000).
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1
  • 13
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau, O. & Tschopp, J. 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
  • 14
    • 4444341939 scopus 로고    scopus 로고
    • Compartmentalization of TNF receptor 1 signaling: Internalized TNF receptosomes as death signaling vesicles
    • Schneider-Brachert, W. et al. Compartmentalization of TNF receptor 1 signaling: Internalized TNF receptosomes as death signaling vesicles. Immunity 21, 415-428 (2004).
    • (2004) Immunity , vol.21 , pp. 415-428
    • Schneider-Brachert, W.1
  • 15
    • 0037432140 scopus 로고    scopus 로고
    • Structure-function analysis of the A20-binding inhibitor of NF-κ B activation, ABIN-1
    • Heyninck, K., Kreike, M. M. & Beyaert, R. Structure-function analysis of the A20-binding inhibitor of NF-κ B activation, ABIN-1. FEBS Lett. 536, 135-140 (2003).
    • (2003) FEBS Lett , vol.536 , pp. 135-140
    • Heyninck, K.1    Kreike, M.M.2    Beyaert, R.3
  • 16
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea, C. K., Deng, L., Xia, Z. P., Pineda, G. & Chen, Z. J. Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 22, 245-257 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 17
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation
    • Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. & Ashwell, J. D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation. Nature Cell Biol. 8, 398-406 (2006).
    • (2006) Nature 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
  • 18
    • 44649166613 scopus 로고    scopus 로고
    • Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins
    • Wagner, S. et al. Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins. Oncogene 27, 3739-3745 (2008).
    • (2008) Oncogene , vol.27 , pp. 3739-3745
    • Wagner, S.1
  • 19
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L. et al. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351-361 (2000).
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1
  • 20
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang, C. et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412, 346-351 (2001).
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1
  • 21
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-κB pathway
    • Chen, Z. J. Ubiquitin signalling in the NF-κB pathway. Nature Cell Biol. 7, 758-765 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 22
    • 44749093460 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of TNFR1 signaling
    • Wertz, I. E. & Dixit, V. M. 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
  • 23
    • 0038510204 scopus 로고    scopus 로고
    • Regulation of apoptosis by ubiquitination
    • Lee, J. C. & Peter, M. E. Regulation of apoptosis by ubiquitination. Immunol. Rev. 193, 39-47 (2003).
    • (2003) Immunol. Rev , vol.193 , pp. 39-47
    • Lee, J.C.1    Peter, M.E.2
  • 24
    • 5444223519 scopus 로고    scopus 로고
    • The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses
    • Boone, D. L. et al. The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses. Nature Immunol. 5, 1052-1060 (2004).
    • (2004) Nature Immunol , vol.5 , pp. 1052-1060
    • Boone, D.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.