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Volumn 481, Issue 7380, 2012, Pages 204-210

Cysteine methylation disrupts ubiquitin-chain sensing in NF-κB activation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; METHYLTRANSFERASE; PROTEIN NLEE; S ADENOSYLMETHIONINE; TAB2 PROTEIN; TAB3 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 84855764312     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10690     Document Type: Article
Times cited : (161)

References (35)
  • 1
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles inNF-kBsignaling
    • Hayden, M. S.&Ghosh, S.Shared principles inNF-kBsignaling. Cell 132, 344-362 (2008).
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 2
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-kB transcription factors in the immune system
    • Vallabhapurapu, S. & Karin, M. Regulation and function of NF-kB transcription factors in the immune system. Annu. Rev. Immunol. 27, 693-733 (2009).
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 3
    • 35348992048 scopus 로고    scopus 로고
    • Manipulation of host-cell pathways by bacterial pathogens
    • DOI 10.1038/nature06247, PII NATURE06247
    • Bhavsar, A. P., Guttman, J. A. & Finlay, B. B. Manipulation of host-cell pathways by bacterial pathogens. Nature 449, 827-834 (2007). (Pubitemid 47598623)
    • (2007) Nature , vol.449 , Issue.7164 , pp. 827-834
    • Bhavsar, A.P.1    Guttman, J.A.2    Finlay, B.B.3
  • 4
    • 35648987280 scopus 로고    scopus 로고
    • Pathogen subversion of cell-intrinsic innate immunity
    • DOI 10.1038/ni1528, PII NI1528
    • Roy, C. R. & Mocarski, E. S. Pathogen subversion of cell-intrinsic innate immunity. Nature Immunol. 8, 1179-1187 (2007). (Pubitemid 350019233)
    • (2007) Nature Immunology , vol.8 , Issue.11 , pp. 1179-1187
    • Roy, C.R.1    Mocarski, E.S.2
  • 6
    • 67650744586 scopus 로고    scopus 로고
    • The role of ubiquitin inNF-kBregulatory pathways
    • Skaug, B., Jiang, X.& Chen, Z. J. The role of ubiquitin inNF-kBregulatory pathways. Annu. Rev. Biochem. 78, 769-796 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 769-796
    • Skaug, B.1    Jiang, X.2    Chen, Z.J.3
  • 7
    • 80053337001 scopus 로고    scopus 로고
    • Biochemistry and cell signaling taught by bacterial effectors
    • Cui, J. & Shao, F. Biochemistry and cell signaling taught by bacterial effectors. Trends Biochem. Sci. 36, 532-540 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 532-540
    • Cui, J.1    Shao, F.2
  • 8
    • 77649216223 scopus 로고    scopus 로고
    • The type III secretion effector NleE inhibits NF-kB activation
    • Nadler, C. et al. The type III secretion effector NleE inhibits NF-kB activation. PLoS Pathog. 6, e1000743 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Nadler, C.1
  • 9
    • 77954066144 scopus 로고    scopus 로고
    • The type III effectors NleE and NleB from enteropathogenic E. coli and OspZ from Shigella block nuclear translocation of NF-kB p65
    • Newton, H. J. et al. The type III effectors NleE and NleB from enteropathogenic E. coli and OspZ from Shigella block nuclear translocation of NF-kB p65. PLoS Pathog. 6, e1000898 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Newton, H.J.1
  • 10
    • 77958133862 scopus 로고    scopus 로고
    • Inhibition of NF-kB signaling in human dendritic cells by the enteropathogenic Escherichia coli effector protein NleE
    • Vossenkämper, A. et al. Inhibition of NF-kB signaling in human dendritic cells by the enteropathogenic Escherichia coli effector protein NleE. J. Immunol. 185, 4118-4127 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 4118-4127
    • Vossenkämper, A.1
  • 12
    • 1542314841 scopus 로고    scopus 로고
    • TAB3, a new binding partner of the protein kinase TAK1
    • DOI 10.1042/BJ20031794
    • Cheung, P. C.,Nebreda, A. R.&Cohen, P.TAB3, a newbinding partner of the protein kinase TAK1. Biochem. J. 378, 27-34 (2004). (Pubitemid 38299541)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 27-34
    • Cheung, P.C.F.1    Nebreda, A.R.2    Cohen, P.3
  • 13
    • 10744220155 scopus 로고    scopus 로고
    • Identification of a human NF-kB-activating protein
    • Jin, G. et al. Identification of a human NF-kB-activating protein, TAB3. Proc. Natl Acad. Sci. USA 101, 2028-2033 (2004).
    • (2004) TAB3. Proc. Natl Acad. Sci. USA , vol.101 , pp. 2028-2033
    • Jin, G.1
  • 14
    • 14844295421 scopus 로고    scopus 로고
    • Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-β-activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding protein TAB1 and TAB2
    • DOI 10.1074/jbc.M407537200
    • Singhirunnusorn, P., Suzuki, S., Kawasaki, N., Saiki, I. & Sakurai, H. Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-b-activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding protein TAB1 and TAB2. J. Biol. Chem. 280, 7359-7368 (2005). (Pubitemid 40341294)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 7359-7368
    • Singhirunnusorn, P.1    Suzuki, S.2    Kawasaki, N.3    Saiki, I.4    Sakurai, H.5
  • 17
    • 72449162040 scopus 로고    scopus 로고
    • Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3
    • Sato, Y., Yoshikawa, A., Yamashita, M., Yamagata, A. & Fukai, S. Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3. EMBO J. 28, 3903-3909 (2009).
    • (2009) EMBO J. , vol.28 , pp. 3903-3909
    • Sato, Y.1    Yoshikawa, A.2    Yamashita, M.3    Yamagata, A.4    Fukai, S.5
  • 18
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach, B. et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471, 591-596 (2011).
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 19
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-kB activity and apoptosis
    • Ikeda, F. et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-kB activity and apoptosis. Nature 471, 637-641 (2011).
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1
  • 20
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-kB-activating linear ubiquitin chain assembly complex
    • Tokunaga, F. et al. SHARPIN is a component of the NF-kB-activating linear ubiquitin chain assembly complex. Nature 471, 633-636 (2011).
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1
  • 21
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • DOI 10.1016/S0968-0004(03)00090-2
    • Schubert, H. L., Blumenthal, R. M. & Cheng, X. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem. Sci. 28, 329-335 (2003). (Pubitemid 36776296)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 22
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • DOI 10.1093/emboj/cdf579
    • Meyer, H. H., Wang, Y. & Warren, G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 21, 5645-5652 (2002). (Pubitemid 35315264)
    • (2002) EMBO Journal , vol.21 , Issue.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 24
    • 70350020147 scopus 로고    scopus 로고
    • NEMOspecifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
    • Laplantine, E. et al. NEMOspecifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J. 28, 2885-2895 (2009).
    • (2009) EMBO J. , vol.28 , pp. 2885-2895
    • Laplantine, E.1
  • 26
    • 0023893331 scopus 로고
    • Functional domains and methyl acceptor sites of the Escherichia coli Ada protein
    • Sedgwick, B., Robins, P., Totty, N. & Lindahl, T. Functional domains and methyl acceptor sites of the Escherichia coli Ada protein. J. Biol. Chem. 263, 4430-4433 (1988). (Pubitemid 18096626)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.9 , pp. 4430-4433
    • Sedgwick, B.1    Robins, P.2    Totty, N.3    Lindahl, T.4
  • 28
    • 2442603566 scopus 로고    scopus 로고
    • Dissecting the Catalytic Mechanism of Betaine-Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis
    • DOI 10.1021/bi049821x
    • Castro, C. et al. Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. Biochemistry 43, 5341-5351 (2004). (Pubitemid 38620926)
    • (2004) Biochemistry , vol.43 , Issue.18 , pp. 5341-5351
    • Castro, C.1    Gratson, A.A.2    Evans, J.C.3    Jiracek, J.4    Collinsova, M.5    Ludwig, M.L.6    Garrow, T.A.7
  • 30
    • 0031244360 scopus 로고    scopus 로고
    • Enzyme-catalyzed methyl transfers to thiols: The role of zinc
    • Matthews, R. G.& Goulding, C. W. Enzyme-catalyzed methyl transfers to thiols: the role of zinc. Curr. Opin. Chem. Biol. 1, 332-339 (1997). (Pubitemid 127437159)
    • (1997) Current Opinion in Chemical Biology , vol.1 , Issue.3 , pp. 332-339
    • Matthews, R.G.1    Goulding, C.W.2
  • 31
    • 69549133937 scopus 로고    scopus 로고
    • A Legionella type IV effector activates the NF-kB pathway by phosphorylating the IkB family of inhibitors
    • Ge, J. et al. A Legionella type IV effector activates the NF-kB pathway by phosphorylating the IkB family of inhibitors. Proc. Natl Acad. Sci. USA 106, 13725-13730 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13725-13730
    • Ge, J.1
  • 32
    • 33847154642 scopus 로고    scopus 로고
    • The phosphothreonine lyase activity of a bacterial type III effector family
    • DOI 10.1126/science.1138960
    • Li, H. et al. The phosphothreonine lyase activity of a bacterial type III effector family. Science 315, 1000-1003 (2007). (Pubitemid 46281190)
    • (2007) Science , vol.315 , Issue.5814 , pp. 1000-1003
    • Li, H.1    Xu, H.2    Zhou, Y.3    Zhang, J.4    Long, C.5    Li, S.6    Chen, S.7    Zhou, J.-M.8    Shao, F.9
  • 33
    • 78649819208 scopus 로고    scopus 로고
    • Chemical probing reveals insights into the signalingmechanismof inflammasome activation
    • Gong, Y. N. et al. Chemical probing reveals insights into the signalingmechanismof inflammasome activation. Cell Res. 20, 1289-1305 (2010).
    • (2010) Cell Res. , vol.20 , pp. 1289-1305
    • Gong, Y.N.1
  • 34
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • Cui, J. et al. Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Science 329, 1215-1218 (2010).
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1
  • 35
    • 50349102579 scopus 로고    scopus 로고
    • Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T
    • Reyes-Turcu, F. E., Shanks, J. R., Komander, D. & Wilkinson, K. D. Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. J. Biol. Chem. 283, 19581-19592 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 19581-19592
    • Reyes-Turcu, F.E.1    Shanks, J.R.2    Komander, D.3    Wilkinson, K.D.4


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