메뉴 건너뛰기




Volumn 424, Issue 6950, 2003, Pages 793-796

CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; RNA; SKIN;

EID: 0042467558     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01803     Document Type: Article
Times cited : (838)

References (27)
  • 1
    • 18844464056 scopus 로고    scopus 로고
    • Identification of the familial cylindromatosis tumour-suppressor gene
    • Bignell, G. R. et al. Identification of the familial cylindromatosis tumour-suppressor gene. Nature Genet. 25, 160-165 (2000).
    • (2000) Nature Genet. , vol.25 , pp. 160-165
    • Bignell, G.R.1
  • 2
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh, S. & Karin, M. Missing pieces in the NF-κB puzzle. Cell 109, S81-S96 (2002).
    • (2002) Cell , vol.109
    • Ghosh, S.1    Karin, M.2
  • 3
    • 0035286726 scopus 로고    scopus 로고
    • Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia
    • Jain, A. et al. Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia. Nature Immunol. 2, 223-228 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 223-228
    • Jain, A.1
  • 4
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • Wilkinson, K. D. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J. 11, 1245-1256 (1997).
    • (1997) FASEB J. , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 5
    • 0032775933 scopus 로고    scopus 로고
    • Involvement of a novel TNF receptor homologue in hair follicle induction
    • Headon, D. J. & Overbeek, P. A. Involvement of a novel TNF receptor homologue in hair follicle induction. Nature Genet. 22, 370-374 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 370-374
    • Headon, D.J.1    Overbeek, P.A.2
  • 6
    • 0033761628 scopus 로고    scopus 로고
    • Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors
    • Yan, M. et al. Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors. Science 290, 523-527 (2000).
    • (2000) Science , vol.290 , pp. 523-527
    • Yan, M.1
  • 7
    • 0036364572 scopus 로고    scopus 로고
    • Cellular signaling pathways engaged by the Epstein-Barr virus transforming protein LMP1
    • Hatzivassiliou, E. & Mosialos, G. Cellular signaling pathways engaged by the Epstein-Barr virus transforming protein LMP1. Front. Biosci. 7, d319-d329 (2002).
    • (2002) Front. Biosci. , vol.7
    • Hatzivassiliou, E.1    Mosialos, G.2
  • 8
    • 0033198702 scopus 로고    scopus 로고
    • TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses
    • Nguyen, L. T. et al. TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses. Immunity 11, 379-389 (1999).
    • (1999) Immunity , vol.11 , pp. 379-389
    • Nguyen, L.T.1
  • 9
    • 0033561039 scopus 로고    scopus 로고
    • TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling
    • Lomaga, M. A. et al. TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling. Genes Dev. 13, 1015-1024 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1015-1024
    • Lomaga, M.A.1
  • 10
    • 0037022539 scopus 로고    scopus 로고
    • Identification of a novel death domain-containing adaptor molecule for ectodysplasin-A receptor that is mutated in crinkled mice
    • Yan, M. et al. Identification of a novel death domain-containing adaptor molecule for ectodysplasin-A receptor that is mutated in crinkled mice. Curr. Biol. 12, 409-413 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 409-413
    • Yan, M.1
  • 11
    • 0037173095 scopus 로고    scopus 로고
    • TRAF6-deficient mice display hypohidrotic ectodermal dysplasia
    • Naito, A. et al. TRAF6-deficient mice display hypohidrotic ectodermal dysplasia. Proc. Natl Acad. Sci. USA 99, 8766-8771 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8766-8771
    • Naito, A.1
  • 12
    • 0029785204 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor associated factor 2 is a mediator of NF-κB activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein
    • Kaye, K. M. et al. Tumor necrosis factor receptor associated factor 2 is a mediator of NF-κB activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein. Proc. Natl Acad. Sci. USA 93, 11085-11090 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11085-11090
    • Kaye, K.M.1
  • 13
    • 0035887040 scopus 로고    scopus 로고
    • TRAF 6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1
    • Schultheiss, U. et al. TRAF6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1. EMBO J. 20, 5678-5691 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5678-5691
    • Schultheiss, U.1
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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 Ubcl3-Uev1A/TNF receptor-associated factor 2 (TRAF2)
    • Shi, C. S. & Kehrl, J. H. Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubcl3-Uev1A/TNF receptor-associated factor 2 (TRAF2). J. Biol. Chem. 278, 15429-15434 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 15429-15434
    • Shi, C.S.1    Kehrl, J.H.2
  • 17
    • 0038579251 scopus 로고    scopus 로고
    • An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc 13. The structural basis for lysine 63 chain catalysis
    • McKenna, S. et al. An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13. The structural basis for lysine 63 chain catalysis. J. Biol. Chem 278, 13151-13158 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 13151-13158
    • McKenna, S.1
  • 18
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin, A. et al. The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12, 419-429 (2000).
    • (2000) Immunity , vol.12 , pp. 419-429
    • Devin, A.1
  • 19
    • 0035021123 scopus 로고    scopus 로고
    • The α and β subunits of IκB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF
    • Devin, A. et al. The α and β subunits of IκB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol. Cell. Biol. 21, 3986-3994 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3986-3994
    • Devin, A.1
  • 20
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation
    • Zhang, S. Q., Kovalenko, A., Cantarella, G. & Wallach, D. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation. Immunity 12, 301-311 (2000).
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 21
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu, M. et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054 (2002).
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1
  • 22
    • 0036546501 scopus 로고    scopus 로고
    • NF-κB in cancer: From innocent bystander to major culprit
    • Karin, M., Cao, Y., Greten, F. R. & Li, Z. W. NF-κB in cancer: from innocent bystander to major culprit. Nature Rev. Cancer 2, 301-310 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.W.4
  • 23
    • 0042467554 scopus 로고    scopus 로고
    • Loss of cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB
    • Brummelkamp, T. R., Nijman, S. M. B., Dirac, A. M. G. & Bernards, R. Loss of cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB. Nature 424, 797-801 (2003).
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.B.2    Dirac, A.M.G.3    Bernards, R.4
  • 24
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP 1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos, G. et al. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 80, 389-399 (1995).
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1
  • 25
    • 0028987479 scopus 로고
    • Stimulation of NF-κB-mediated transcription by mutant derivatives of the latent membrane protein of Epstein-Barr virus
    • Mitchell, T. & Sugden, B. Stimulation of NF-κB-mediated transcription by mutant derivatives of the latent membrane protein of Epstein-Barr virus. J. Virol. 69, 2968-2976 (1995).
    • (1995) J. Virol. , vol.69 , pp. 2968-2976
    • Mitchell, T.1    Sugden, B.2
  • 26
    • 0030838845 scopus 로고    scopus 로고
    • Ultraspiracle, a Drosophila retinoic X receptor α homologue, can mobilize the human thyroid hormone receptor to transactivate a human promoter
    • Hatzivassiliou, E., Cardot, P., Zannis, V. I. & Mitsialis, S. A. Ultraspiracle, a Drosophila retinoic X receptor α homologue, can mobilize the human thyroid hormone receptor to transactivate a human promoter. Biochemistry 36, 9221-9231 (1997).
    • (1997) Biochemistry , vol.36 , pp. 9221-9231
    • Hatzivassiliou, E.1    Cardot, P.2    Zannis, V.I.3    Mitsialis, S.A.4
  • 27
    • 0029956392 scopus 로고    scopus 로고
    • Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: Role in NF-κB activation
    • Devergne, O. et al. Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-κB activation. Mol. Cell. Biol. 16, 7098-7108 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7098-7108
    • Devergne, O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.