메뉴 건너뛰기




Volumn 52, Issue 51, 2013, Pages 9141-9154

Mutation of nonessential cysteines shows that the NF-κB essential modulator forms a constitutive noncovalent dimer that binds IκB kinase-β with high affinity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CELL CULTURE; CELL DEATH; COVALENT BONDS; ENZYMES;

EID: 84895776854     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401368r     Document Type: Article
Times cited : (16)

References (58)
  • 1
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-κB: Players, pathways, perspectives
    • Gilmore, T. D. (2006) Introduction to NF-κB: Players, pathways, perspectives Oncogene 25, 6680-6684
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 2
    • 0032541657 scopus 로고    scopus 로고
    • IKKγ is an essential regulatory subunit of the IκB kinase complex
    • Rothwarf, D. M., Zandi, E., Natoli, G., and Karin, M. (1998) IKKγ is an essential regulatory subunit of the IκB kinase complex Nature 395, 297-300
    • (1998) Nature , vol.395 , pp. 297-300
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 3
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., and Karin, M. (1997) A cytokine-responsive IκB kinase that activates the transcription factor NF-κB Nature 388, 548-554
    • (1997) Nature , vol.388 , pp. 548-554
    • Didonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 4
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation
    • Yamaoka, S., Courtois, G., Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H. E., Kay, R. J., and Israël, A. (1998) Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation Cell 93, 1231-1240
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6    Kirk, H.E.7    Kay, R.J.8    Israël, A.9
  • 5
    • 0033996762 scopus 로고    scopus 로고
    • The IκB kinase (IKK) and NF-κB: Key elements of proinflammatory signalling
    • Karin, M. and Delhase, M. (2000) The IκB kinase (IKK) and NF-κB: Key elements of proinflammatory signalling Semin. Immunol. 12, 85-98
    • (2000) Semin. Immunol. , vol.12 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 6
    • 78650907445 scopus 로고    scopus 로고
    • A single NFκB system for both canonical and non-canonical signaling
    • Shih, V. F.-S., Tsui, R., Caldwell, A., and Hoffmann, A. (2010) A single NFκB system for both canonical and non-canonical signaling Cell Res. 21, 86-102
    • (2010) Cell Res. , vol.21 , pp. 86-102
    • Shih, V.F.-S.1    Tsui, R.2    Caldwell, A.3    Hoffmann, A.4
  • 7
    • 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
  • 9
    • 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
  • 10
    • 84863621364 scopus 로고    scopus 로고
    • Analysis of 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 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, 13626-12634
    • (2012) J. Biol. Chem. , vol.287 , pp. 13626-12634
    • Kensche, T.1    Tokunaga, F.2    Ikeda, F.3    Goto, E.4    Iwai, K.5    Dikic, I.6
  • 15
    • 33750454819 scopus 로고    scopus 로고
    • Mutations in the NF-κB signaling pathway: Implications for human disease
    • Courtois, G. and Gilmore, T. D. (2006) Mutations in the NF-κB signaling pathway: Implications for human disease Oncogene 25, 6831-6843
    • (2006) Oncogene , vol.25 , pp. 6831-6843
    • Courtois, G.1    Gilmore, T.D.2
  • 16
    • 0034284715 scopus 로고    scopus 로고
    • Selective inhibition of NF-κB activation by a peptide that blocks the interaction of NEMO with the IκB kinase complex
    • May, M. J., D'Acquisto, F., Madge, L. A., Glockner, J., Pober, J. S., and Ghosh, S. (2000) Selective inhibition of NF-κB activation by a peptide that blocks the interaction of NEMO with the IκB kinase complex Science 289, 1550-1554
    • (2000) Science , vol.289 , pp. 1550-1554
    • May, M.J.1    D'Acquisto, F.2    Madge, L.A.3    Glockner, J.4    Pober, J.S.5    Ghosh, S.6
  • 17
    • 0141621240 scopus 로고    scopus 로고
    • A role for NF-κB essential modifier/IκB kinase-γ (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α
    • Tang, E. D. (2003) A role for NF-κB essential modifier/IκB kinase-γ (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α J. Biol. Chem. 278, 37297-37305
    • (2003) J. Biol. Chem. , vol.278 , pp. 37297-37305
    • Tang, E.D.1
  • 18
    • 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., and Chen, Z. J. (2006) Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO Mol. Cell 22, 245-257
    • (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
  • 19
    • 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
  • 20
    • 33750312876 scopus 로고    scopus 로고
    • Posttranslational modifications of NEMO and its partners in NF-κB signaling
    • Sebban, H., Yamaoka, S., and Courtois, G. (2006) Posttranslational modifications of NEMO and its partners in NF-κB signaling Trends Cell Biol. 16, 569-577
    • (2006) Trends Cell Biol. , vol.16 , pp. 569-577
    • Sebban, H.1    Yamaoka, S.2    Courtois, G.3
  • 21
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress
    • Huang, T. T., Wuerzberger-Davis, S. M., Wu, Z.-H., and Miyamoto, S. (2003) Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress Cell 115, 565-576
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.-H.3    Miyamoto, S.4
  • 25
    • 77955094923 scopus 로고    scopus 로고
    • A homogeneous time-resolved fluorescence-based high-throughput screening system for discovery of inhibitors of IKKβ-NEMO interaction
    • Gotoh, Y., Nagata, H., Kase, H., Shimonishi, M., and Ido, M. (2010) A homogeneous time-resolved fluorescence-based high-throughput screening system for discovery of inhibitors of IKKβ-NEMO interaction Anal. Biochem. 405, 19-27
    • (2010) Anal. Biochem. , vol.405 , pp. 19-27
    • Gotoh, Y.1    Nagata, H.2    Kase, H.3    Shimonishi, M.4    Ido, M.5
  • 27
    • 0037145860 scopus 로고    scopus 로고
    • Stimulation of IKK-γ oligomerization by the human T-cell leukemia virus oncoprotein Tax
    • Huang, G. J., Zhang, Z. Q., and Jin, D. Y. (2002) Stimulation of IKK-γ oligomerization by the human T-cell leukemia virus oncoprotein Tax FEBS Lett. 531, 494-498
    • (2002) FEBS Lett. , vol.531 , pp. 494-498
    • Huang, G.J.1    Zhang, Z.Q.2    Jin, D.Y.3
  • 29
    • 0037195419 scopus 로고    scopus 로고
    • Characterization of the IκB-kinase NEMO binding domain
    • May, M. J. (2002) Characterization of the IκB-kinase NEMO binding domain J. Biol. Chem. 277, 45992-46000
    • (2002) J. Biol. Chem. , vol.277 , pp. 45992-46000
    • May, M.J.1
  • 33
    • 70349995780 scopus 로고    scopus 로고
    • Crystal structure of the NEMO ubiquitin-binding domain in complex with Lys 63-linked di-ubiquitin
    • Yoshikawa, A., Sato, Y., Yamashita, M., Mimura, H., Yamagata, A., and Fukai, S. (2009) Crystal structure of the NEMO ubiquitin-binding domain in complex with Lys 63-linked di-ubiquitin FEBS Lett. 583, 3317-3322
    • (2009) FEBS Lett. , vol.583 , pp. 3317-3322
    • Yoshikawa, A.1    Sato, Y.2    Yamashita, M.3    Mimura, H.4    Yamagata, A.5    Fukai, S.6
  • 34
    • 3142546430 scopus 로고    scopus 로고
    • The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains
    • Agou, F., Traincard, F., Vinolo, E., Courtois, G., Yamaoka, S., Israël, A., and Véron, M. (2004) The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains J. Biol. Chem. 279, 27861-27869
    • (2004) J. Biol. Chem. , vol.279 , pp. 27861-27869
    • Agou, F.1    Traincard, F.2    Vinolo, E.3    Courtois, G.4    Yamaoka, S.5    Israël, A.6    Véron, M.7
  • 40
    • 11144265736 scopus 로고    scopus 로고
    • A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization
    • Roehrl, M. H. A., Wang, J. Y., and Wagner, G. (2004) A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization Biochemistry 43, 16056-16066
    • (2004) Biochemistry , vol.43 , pp. 16056-16066
    • Roehrl, M.H.A.1    Wang, J.Y.2    Wagner, G.3
  • 41
    • 13544261427 scopus 로고    scopus 로고
    • Selectivity of BAFF/BLyS and APRIL for binding to the TNF family receptors BAFFR/BR3 and BCMA
    • Day, E. S., Cachero, T. G., Qian, F., Sun, Y., Wen, D., Pelletier, M., Hsu, Y.-M., and Whitty, A. (2005) Selectivity of BAFF/BLyS and APRIL for binding to the TNF family receptors BAFFR/BR3 and BCMA Biochemistry 44, 1919-1931
    • (2005) Biochemistry , vol.44 , pp. 1919-1931
    • Day, E.S.1    Cachero, T.G.2    Qian, F.3    Sun, Y.4    Wen, D.5    Pelletier, M.6    Hsu, Y.-M.7    Whitty, A.8
  • 42
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmič, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase Anal. Biochem. 237, 260-273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmič, P.1
  • 43
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N. J. (2007) Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 1, 2876-2890
    • (2007) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 44
    • 0035283168 scopus 로고    scopus 로고
    • SOMCD: Method for evaluating protein secondary structure from UV circular dichroism spectra
    • Unneberg, P., Merelo, J. J., Chacón, P., and Morán, F. (2001) SOMCD: Method for evaluating protein secondary structure from UV circular dichroism spectra Proteins: Struct., Funct., Bioinf. 42, 460-470
    • (2001) Proteins: Struct., Funct., Bioinf. , vol.42 , pp. 460-470
    • Unneberg, P.1    Merelo, J.J.2    Chacón, P.3    Morán, F.4
  • 45
    • 31044445246 scopus 로고    scopus 로고
    • Inhibition of transcription factor NF-κB signaling proteins IKKβ and p65 through specific cysteine residues by epoxyquinone A monomer: Correlation with its anti-cancer cell growth activity
    • Liang, M.-C., Bardhan, S., Pace, E. A., Rosman, D., Beutler, J. A., Porco, J. A., Jr., and Gilmore, T. D. (2006) Inhibition of transcription factor NF-κB signaling proteins IKKβ and p65 through specific cysteine residues by epoxyquinone A monomer: Correlation with its anti-cancer cell growth activity Biochem. Pharmacol. 71, 634-645
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 634-645
    • Liang, M.-C.1    Bardhan, S.2    Pace, E.A.3    Rosman, D.4    Beutler, J.A.5    Porco, Jr.J.A.6    Gilmore, T.D.7
  • 46
    • 0037061742 scopus 로고    scopus 로고
    • Immortalized embryonic mouse fibroblasts lacking the RelA subunit of transcription factor NF-κB have a malignantly transformed phenotype
    • Gapuzan, M.-E. R., Yufit, P. V., and Gilmore, T. D. (2002) Immortalized embryonic mouse fibroblasts lacking the RelA subunit of transcription factor NF-κB have a malignantly transformed phenotype Oncogene 21, 2484-2492
    • (2002) Oncogene , vol.21 , pp. 2484-2492
    • Gapuzan, M.-E.R.1    Yufit, P.V.2    Gilmore, T.D.3
  • 48
    • 0029026723 scopus 로고
    • Active-site titration of peptidases
    • Knight, C. G. (1995) Active-site titration of peptidases Methods Enzymol. 248, 85-101
    • (1995) Methods Enzymol. , vol.248 , pp. 85-101
    • Knight, C.G.1
  • 49
    • 84879807263 scopus 로고    scopus 로고
    • Determining the affinity and stoichiometry of interactions between unmodified proteins in solution using biacore
    • Day, E. S., Capili, A. D., Borysenko, C. W., Zafari, M., and Whitty, A. (2013) Determining the affinity and stoichiometry of interactions between unmodified proteins in solution using biacore Anal. Biochem. 440, 96-107
    • (2013) Anal. Biochem. , vol.440 , pp. 96-107
    • Day, E.S.1    Capili, A.D.2    Borysenko, C.W.3    Zafari, M.4    Whitty, A.5
  • 50
    • 0031027480 scopus 로고    scopus 로고
    • Assessment of affinity constants by rapid solid phase detection of equilibrium binding in a flow system
    • Piehler, J., Brecht, A., Giersch, T., Hock, B., and Gauglitz, G. (1997) Assessment of affinity constants by rapid solid phase detection of equilibrium binding in a flow system J. Immunol. Methods 201, 189-206
    • (1997) J. Immunol. Methods , vol.201 , pp. 189-206
    • Piehler, J.1    Brecht, A.2    Giersch, T.3    Hock, B.4    Gauglitz, G.5
  • 51
    • 33845428995 scopus 로고    scopus 로고
    • Dimerization of the IκB kinase-binding domain of NEMO is required for tumor necrosis factor α-induced NF-κB activity
    • Marienfeld, R. B., Palkowitsch, L., and Ghosh, S. (2006) Dimerization of the IκB kinase-binding domain of NEMO is required for tumor necrosis factor α-induced NF-κB activity Mol. Cell. Biol. 26, 9209-9219
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9209-9219
    • Marienfeld, R.B.1    Palkowitsch, L.2    Ghosh, S.3
  • 53
    • 34247560784 scopus 로고    scopus 로고
    • NEMO oligomerization in the dynamic assembly of the IκB kinase core complex
    • Fontan, E., Traincard, F., Levy, S. G., Yamaoka, S., Véron, M., and Agou, F. (2007) NEMO oligomerization in the dynamic assembly of the IκB kinase core complex FEBS J. 274, 2540-2551
    • (2007) FEBS J. , vol.274 , pp. 2540-2551
    • Fontan, E.1    Traincard, F.2    Levy, S.G.3    Yamaoka, S.4    Véron, M.5    Agou, F.6
  • 54
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield, N. J. (2007) Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions Nat. Protoc. 1, 2527-2535
    • (2007) Nat. Protoc. , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 55
    • 0033367229 scopus 로고    scopus 로고
    • Oligomeric state of wild-type and cysteine-less yeast mitochondrial citrate transport proteins
    • Kotaria, R., Mayor, J. A., Walters, D. E., and Kaplan, R. S. (1999) Oligomeric state of wild-type and cysteine-less yeast mitochondrial citrate transport proteins J. Bioenerg. Biomembr. 31, 543-549
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 543-549
    • Kotaria, R.1    Mayor, J.A.2    Walters, D.E.3    Kaplan, R.S.4
  • 56
    • 0037332580 scopus 로고    scopus 로고
    • Tetrameric oligomerization of IκB kinase (IKKγ) is obligatory for IKK complex activity and NF-κB activation
    • Tegethoff, S., Behlke, J., and Scheidereit, C. (2003) Tetrameric oligomerization of IκB kinase (IKKγ) is obligatory for IKK complex activity and NF-κB activation Mol. Cell. Biol. 23, 2029-2041
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2029-2041
    • Tegethoff, S.1    Behlke, J.2    Scheidereit, C.3
  • 57
    • 71749083630 scopus 로고    scopus 로고
    • Impediment of NEMO oligomerization inhibits osteoclastogenesis and osteolysis
    • Darwech, I., Otero, J., Alhawagri, M., Dai, S., and Abu-Amer, Y. (2009) Impediment of NEMO oligomerization inhibits osteoclastogenesis and osteolysis J. Cell. Biochem. 108, 1337-1345
    • (2009) J. Cell. Biochem. , vol.108 , pp. 1337-1345
    • Darwech, I.1    Otero, J.2    Alhawagri, M.3    Dai, S.4    Abu-Amer, Y.5
  • 58
    • 84874724662 scopus 로고    scopus 로고
    • Update on activities at the Universal Protein Resource (UniProt) in 2013
    • The UniProt Consortium () - D47
    • The UniProt Consortium (2012) Update on activities at the Universal Protein Resource (UniProt) in 2013 Nucleic Acids Res. 41, D43-D47
    • (2012) Nucleic Acids Res. , vol.41 , pp. 43


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.