메뉴 건너뛰기




Volumn 288, Issue 47, 2013, Pages 33722-33737

Two-sided ubiquitin binding of NF-κB essential modulator (NEMO) zinc finger unveiled by a mutation associated with anhidrotic ectodermal dysplasia with immunodeficiency syndrome

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; BINDING PROPERTIES; C-TERMINAL DOMAINS; IMMUNODEFICIENCY SYNDROMES; PATHOGENIC MUTATION; POINT MUTATIONS; SEDIMENTATION VELOCITIES; STRUCTURAL MODELING;

EID: 84888349683     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.483305     Document Type: Article
Times cited : (10)

References (52)
  • 1
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century. Remarkable progress and outstanding questions
    • Hayden, M. S., and Ghosh, S. (2012) NF-κB, the first quarter-century. Remarkable progress and outstanding questions. Genes Dev. 26, 203-234
    • (2012) Genes Dev. , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 6
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia, Z. P., Sun, L., Chen, X., Pineda, G., Jiang, X., Adhikari, A., Zeng, W., and Chen, Z. J. (2009) Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 461, 114-119
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1    Sun, L.2    Chen, X.3    Pineda, G.4    Jiang, X.5    Adhikari, A.6    Zeng, W.7    Chen, Z.J.8
  • 8
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • Wu, H. (2013) Higher-order assemblies in a new paradigm of signal transduction. Cell 153, 287-292
    • (2013) Cell , vol.153 , pp. 287-292
    • Wu, H.1
  • 10
    • 0036724051 scopus 로고    scopus 로고
    • The carboxyl-terminal region of IκB kinase γ (IKKγ) is required for full IKK activation
    • Makris, C., Roberts, J. L., and Karin, M. (2002) The carboxyl-terminal region of IκB kinase γ (IKKγ) is required for full IKK activation. Mol. Cell. Biol. 22, 6573-6581
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6573-6581
    • Makris, C.1    Roberts, J.L.2    Karin, M.3
  • 11
    • 0036315743 scopus 로고    scopus 로고
    • The zinc finger domain of NEMO is selectively required for NF-κB activation by UV radiation and topoisomerase inhibitors
    • Huang, T. T., Feinberg, S. L., Suryanarayanan, S., and Miyamoto, S. (2002) The zinc finger domain of NEMO is selectively required for NF-κB activation by UV radiation and topoisomerase inhibitors. Mol. Cell. Biol. 22, 5813-5825
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5813-5825
    • Huang, T.T.1    Feinberg, S.L.2    Suryanarayanan, S.3    Miyamoto, S.4
  • 12
    • 70350020147 scopus 로고    scopus 로고
    • NEMO specifically recognizes Lys-63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
    • Laplantine, E., Fontan, E., Chiaravalli, J., Lopez, T., Lakisic, G., Véron, M., Agou, F., and Israël, A. (2009) NEMO specifically recognizes Lys-63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J. 28, 2885-2895
    • (2009) EMBO J. , vol.28 , pp. 2885-2895
    • Laplantine, E.1    Fontan, E.2    Chiaravalli, J.3    Lopez, T.4    Lakisic, G.5    Véron, M.6    Agou, F.7    Israël, A.8
  • 14
    • 40849140675 scopus 로고    scopus 로고
    • Solution structure of NEMO zinc-finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation
    • Cordier, F., Vinolo, E., Véron, M., Delepierre, M., and Agou, F. (2008) Solution structure of NEMO zinc-finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation. J. Mol. Biol. 377, 1419-1432
    • (2008) J. Mol. Biol. , vol.377 , pp. 1419-1432
    • Cordier, F.1    Vinolo, E.2    Véron, M.3    Delepierre, M.4    Agou, F.5
  • 16
    • 33847338933 scopus 로고    scopus 로고
    • Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase η
    • Bomar, M. G., Pai, M. T., Tzeng, S. R., Li, S. S., and Zhou, P. (2007) Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase η. EMBO Rep. 8, 247-251
    • (2007) EMBO Rep. , vol.8 , pp. 247-251
    • Bomar, M.G.1    Pai, M.T.2    Tzeng, S.R.3    Li, S.S.4    Zhou, P.5
  • 17
  • 18
    • 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., and Fukai, S. (2009) Structural basis for specific recognition of Lys-63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3. EMBO J. 28, 3903-3909
    • (2009) EMBO J. , vol.28 , pp. 3903-3909
    • Sato, Y.1    Yoshikawa, A.2    Yamashita, M.3    Yamagata, A.4    Fukai, S.5
  • 21
    • 84867062977 scopus 로고    scopus 로고
    • A20 inhibits LUBAC-mediated NF-κB activation by binding linear polyubiquitin chains via its zinc finger 7
    • Verhelst, K., Carpentier, I., Kreike, M., Meloni, L., Verstrepen, L., Kensche, T., Dikic, I., and Beyaert, R. (2012) A20 inhibits LUBAC-mediated NF-κB activation by binding linear polyubiquitin chains via its zinc finger 7. EMBO J. 31, 3845-3855
    • (2012) EMBO J. , vol.31 , pp. 3845-3855
    • Verhelst, K.1    Carpentier, I.2    Kreike, M.3    Meloni, L.4    Verstrepen, L.5    Kensche, T.6    Dikic, I.7    Beyaert, R.8
  • 25
    • 80053956525 scopus 로고    scopus 로고
    • Direct inhibition of NF-κB activation by peptide targeting the NOA ubiquitin binding domain of NEMO
    • Chiaravalli, J., Fontan, E., Fsihi, H., Coic, Y. M., Baleux, F., Véron, M., and Agou, F. (2011) Direct inhibition of NF-κB activation by peptide targeting the NOA ubiquitin binding domain of NEMO. Biochem. Pharmacol. 82, 1163-1174
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1163-1174
    • Chiaravalli, J.1    Fontan, E.2    Fsihi, H.3    Coic, Y.M.4    Baleux, F.5    Véron, M.6    Agou, F.7
  • 27
    • 0034624810 scopus 로고    scopus 로고
    • Somatic mutagenesis studies of NF-κB signaling in human T cells. Evidence for an essential role of IKK κ in NF-κB activation by T-cell costimulatory signals and HTLV-I Tax protein
    • Harhaj, E. W., Good, L., Xiao, G., Uhlik, M., Cvijic, M. E., Rivera-Walsh, I., and Sun, S. C. (2000) Somatic mutagenesis studies of NF-κB signaling in human T cells. Evidence for an essential role of IKK κ in NF-κB activation by T-cell costimulatory signals and HTLV-I Tax protein. Oncogene 19, 1448-1456
    • (2000) Oncogene , vol.19 , pp. 1448-1456
    • Harhaj, E.W.1    Good, L.2    Xiao, G.3    Uhlik, M.4    Cvijic, M.E.5    Rivera-Walsh, I.6    Sun, S.C.7
  • 28
    • 33646548319 scopus 로고    scopus 로고
    • A point mutation in NEMO associated with anhidrotic ectodermal dysplasia with immunodeficiency pathology results in destabilization of the oligomer and reduces lipopolysaccharide- and tumor necrosis factor-mediated NF-κB activation
    • Vinolo, E., Sebban, H., Chaffotte, A., Israël, A., Courtois, G., Véron, M., and Agou, F. (2006) A point mutation in NEMO associated with anhidrotic ectodermal dysplasia with immunodeficiency pathology results in destabilization of the oligomer and reduces lipopolysaccharide- and tumor necrosis factor-mediated NF-κB activation. J. Biol. Chem. 281, 6334-6348
    • (2006) J. Biol. Chem. , vol.281 , pp. 6334-6348
    • Vinolo, E.1    Sebban, H.2    Chaffotte, A.3    Israël, A.4    Courtois, G.5    Véron, M.6    Agou, F.7
  • 29
    • 39549106692 scopus 로고    scopus 로고
    • The structure of the CYLDUSP domain explains its specificity for Lys-63-linked polyubiquitin and reveals a B box module
    • Komander, D., Lord, C. J., Scheel, H., Swift, S., Hofmann, K., Ashworth, A., and Barford, D. (2008) The structure of the CYLDUSP domain explains its specificity for Lys-63-linked polyubiquitin and reveals a B box module. Mol. Cell 29, 451-464
    • (2008) Mol. Cell , vol.29 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3    Swift, S.4    Hofmann, K.5    Ashworth, A.6    Barford, D.7
  • 30
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown, P. H., and Schuck, P. (2006) Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys. J. 90, 4651-4661
    • (2006) Biophys. J. , vol.90 , pp. 4651-4661
    • Brown, P.H.1    Schuck, P.2
  • 32
    • 80054950096 scopus 로고    scopus 로고
    • Biophysical analysis of the interaction of toxic metal ions and oxidants with the zinc finger domain of XPA
    • Hartwig, A., Schwerdtle, T., and Bal, W. (2010) Biophysical analysis of the interaction of toxic metal ions and oxidants with the zinc finger domain of XPA. Methods Mol. Biol. 649, 399-410
    • (2010) Methods Mol. Biol. , vol.649 , pp. 399-410
    • Hartwig, A.1    Schwerdtle, T.2    Bal, W.3
  • 33
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCKweb server for data-driven biomolecular docking
    • De Vries, S. J., Van Dijk, M., and Bonvin, A. M. (2010) The HADDOCKweb server for data-driven biomolecular docking. Nat. Protoc. 5, 883-897
    • (2010) Nat. Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.3
  • 34
    • 0035286726 scopus 로고    scopus 로고
    • Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia
    • Jain, A., Ma, C. A., Liu, S., Brown, M., Cohen, J., and Strober, W. (2001) Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia. Nat. Immunol. 2, 223-228
    • (2001) Nat. Immunol. , vol.2 , pp. 223-228
    • Jain, A.1    Ma, C.A.2    Liu, S.3    Brown, M.4    Cohen, J.5    Strober, W.6
  • 35
    • 39149094918 scopus 로고    scopus 로고
    • Mutations in the zinc finger domain of IKKγ block the activation of NF-κB and the induction of IL-2 in stimulated T lymphocytes
    • Shifera, A. S., and Horwitz, M. S. (2008) Mutations in the zinc finger domain of IKKγ block the activation of NF-κB and the induction of IL-2 in stimulated T lymphocytes. Mol. Immunol. 45, 1633-1645
    • (2008) Mol. Immunol. , vol.45 , pp. 1633-1645
    • Shifera, A.S.1    Horwitz, M.S.2
  • 41
    • 0842321781 scopus 로고    scopus 로고
    • The zinc finger mutation C417R of I-κB kinase γ impairs lipopolysaccharideand TNF-mediated NF-κ B activation through inhibiting phosphorylation of the I-κ B kinase β activation loop
    • Yang, F., Yamashita, J., Tang, E., Wang, H. L., Guan, K., and Wang, C. Y. (2004) The zinc finger mutation C417R of I-κB kinase γ impairs lipopolysaccharideand TNF-mediated NF-κ B activation through inhibiting phosphorylation of the I-κ B kinase β activation loop. J. Immunol. 172, 2446-2452
    • (2004) J. Immunol. , vol.172 , pp. 2446-2452
    • Yang, F.1    Yamashita, J.2    Tang, E.3    Wang, H.L.4    Guan, K.5    Wang, C.Y.6
  • 42
    • 84863840549 scopus 로고    scopus 로고
    • NEMO ensures signaling specificity of the pleiotropic IKKβ by directing its kinase activity toward IκBα
    • Schröfelbauer, B., Polley, S., Behar, M., Ghosh, G., and Hoffmann, A. (2012) NEMO ensures signaling specificity of the pleiotropic IKKβ by directing its kinase activity toward IκBα. Mol. Cell 47, 111-121
    • (2012) Mol. Cell , vol.47 , pp. 111-121
    • Schröfelbauer, B.1    Polley, S.2    Behar, M.3    Ghosh, G.4    Hoffmann, A.5
  • 43
    • 68249135262 scopus 로고    scopus 로고
    • Avid interactions underlie the Lys-63-linked polyubiquitin binding specificities observed for UBA domains
    • Sims, J. J., Haririnia, A., Dickinson, B. C., Fushman, D., and Cohen, R. E. (2009) Avid interactions underlie the Lys-63-linked polyubiquitin binding specificities observed for UBA domains. Nat. Struct. Mol. Biol. 16, 883-889
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 883-889
    • Sims, J.J.1    Haririnia, A.2    Dickinson, B.C.3    Fushman, D.4    Cohen, R.E.5
  • 44
    • 73649116305 scopus 로고    scopus 로고
    • Exploring the linkage dependence of polyubiquitin conformations using molecular modeling
    • Fushman, D., and Walker, O. (2010) Exploring the linkage dependence of polyubiquitin conformations using molecular modeling. J. Mol. Biol. 395, 803-814
    • (2010) J. Mol. Biol. , vol.395 , pp. 803-814
    • Fushman, D.1    Walker, O.2
  • 46
    • 84857782898 scopus 로고    scopus 로고
    • Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling
    • Sims, J. J., Scavone, F., Cooper, E. M., Kane, L. A., Youle, R. J., Boeke, J. D., and Cohen, R. E. (2012) Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling. Nat. Methods 9, 303-309
    • (2012) Nat. Methods , vol.9 , pp. 303-309
    • Sims, J.J.1    Scavone, F.2    Cooper, E.M.3    Kane, L.A.4    Youle, R.J.5    Boeke, J.D.6    Cohen, R.E.7
  • 47
    • 84863621364 scopus 로고    scopus 로고
    • Analysis of nuclear factor-κB (NF-κB) essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-κB
    • Kensche, T., Tokunaga, F., Ikeda, F., Goto, E., Iwai, K., and Dikic, I. (2012) Analysis of nuclear factor-κB (NF-κB) essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-κB. J. Biol. Chem. 287, 23626-23634
    • (2012) J. Biol. Chem. , vol.287 , pp. 23626-23634
    • Kensche, T.1    Tokunaga, F.2    Ikeda, F.3    Goto, E.4    Iwai, K.5    Dikic, I.6
  • 49
    • 0020452292 scopus 로고
    • Associative properties of the Escherichia coli galactose binding protein and maltose binding protein
    • Richarme, G. (1982) Associative properties of the Escherichia coli galactose binding protein and maltose binding protein. Biochem. Biophys. Res. Commun. 105, 476-481
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 476-481
    • Richarme, G.1
  • 51
    • 62549161305 scopus 로고    scopus 로고
    • Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80
    • Sims, J. J., and Cohen, R. E. (2009) Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80. Mol. Cell 33, 775-783
    • (2009) Mol. Cell , vol.33 , pp. 775-783
    • Sims, J.J.1    Cohen, R.E.2
  • 52
    • 77953027489 scopus 로고    scopus 로고
    • Structure and function of the molecular chaperone Trigger Factor
    • Hoffmann, A., Bukau, B., and Kramer, G. (2010) Structure and function of the molecular chaperone Trigger Factor. Biochim. Biophys. Acta 1803, 650-661
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 650-661
    • Hoffmann, A.1    Bukau, B.2    Kramer, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.