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Volumn 115, Issue 5, 2003, Pages 565-576

Sequential Modification of NEMO/IKKγ by SUMO-1 and Ubiquitin Mediates NF-κB Activation by Genotoxic Stress

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SUMO 1 PROTEIN; UBIQUITIN;

EID: 0344305376     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00895-X     Document Type: Article
Times cited : (501)

References (56)
  • 1
    • 0035449355 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling through the ATM and ATR kinases
    • Abraham R.T. Cell cycle checkpoint signaling through the ATM and ATR kinases. Genes Dev. 15:2001;2177-2196.
    • (2001) Genes Dev. , vol.15 , pp. 2177-2196
    • Abraham, R.T.1
  • 3
    • 0023724778 scopus 로고
    • Iκb: A specific inhibitor of the nf-κb transcription factor
    • Baeuerle P.A., Baltimore D. Iκb. a specific inhibitor of the nf-κb transcription factor Science. 242:1988;540-546.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 4
    • 0037472924 scopus 로고    scopus 로고
    • DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
    • Bakkenist C.J., Kastan M.B. DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature. 421:2003;499-506.
    • (2003) Nature , vol.421 , pp. 499-506
    • Bakkenist, C.J.1    Kastan, M.B.2
  • 5
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB
    • Brummelkamp T.R., Nijman S.M., Dirac A.M., Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB. Nature. 424:2003;797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 6
    • 0141645610 scopus 로고    scopus 로고
    • Transcription factors activated in mammalian cells after clinically relevant doses of ionizing radiation
    • Criswell T., Leskov K., Miyamoto S., Luo G., Boothman D.A. Transcription factors activated in mammalian cells after clinically relevant doses of ionizing radiation. Oncogene. 22:2003;5813-5827.
    • (2003) Oncogene , vol.22 , pp. 5813-5827
    • Criswell, T.1    Leskov, K.2    Miyamoto, S.3    Luo, G.4    Boothman, D.A.5
  • 7
    • 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., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell. 103:2000;351-361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 8
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro J.M., Rodriguez M.S., Hay R.T. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell. 2:1998;233-239.
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 9
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Devary Y., Gottlieb R.A., Smeal T., Karin M. The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell. 71:1992;1081-1091.
    • (1992) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 11
    • 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(Suppl):2002;S81-S96.
    • (2002) Cell , vol.109 , Issue.SUPPL
    • Ghosh, S.1    Karin, M.2
  • 13
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 14
    • 0034960907 scopus 로고    scopus 로고
    • Postrepression activation of NF-κB requires the amino-terminal nuclear export signal specific to IκBα
    • Huang T.T., Miyamoto S. Postrepression activation of NF-κB requires the amino-terminal nuclear export signal specific to IκBα Mol. Cell. Biol. 21:2001;4737-4747.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4737-4747
    • Huang, T.T.1    Miyamoto, S.2
  • 16
    • 0033953587 scopus 로고    scopus 로고
    • A nuclear export signal in the N-terminal regulatory doman of IκBa controls cytoplasmic localization of the inactive NF-κB/IκBa complexes
    • b
    • Huang T.T., Kudo N., Yoshida M., Miyamoto S. A nuclear export signal in the N-terminal regulatory doman of IκBa controls cytoplasmic localization of the inactive NF-κB/IκBa complexes. Proc. Natl. Acad. Sci. USA. 97:2000;1014-1019. b.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1014-1019
    • Huang, T.T.1    Kudo, N.2    Yoshida, M.3    Miyamoto, S.4
  • 17
    • 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., Miyamoto S. The zinc finger domain of NEMO is selectively required for NF-κB activation by UV radiation and topoisomerase inhibitors. Mol. Cell. Biol. 22:2002;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
  • 18
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T. Signaling-2000 and beyond. Cell. 100:2000;113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 19
    • 0037382303 scopus 로고    scopus 로고
    • The death domain kinase RIP has an essential role in DNA damage-induced NF-κB activation
    • Hur G.M., Lewis J., Yang Q., Lin Y., Nakano H., Nedospasov S., Liu Z.G. The death domain kinase RIP has an essential role in DNA damage-induced NF-κB activation. Genes Dev. 17:2003;873-882.
    • (2003) Genes Dev. , vol.17 , pp. 873-882
    • Hur, G.M.1    Lewis, J.2    Yang, Q.3    Lin, Y.4    Nakano, H.5    Nedospasov, S.6    Liu, Z.G.7
  • 20
    • 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., Strober W. Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia. Nat. Immunol. 2:2001;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
  • 21
    • 0029328342 scopus 로고
    • Transcriptional control by protein phosphorylation: Signal transmission from the cell surface to the nucleus
    • Karin M., Hunter T. Transcriptional control by protein phosphorylation. signal transmission from the cell surface to the nucleus Curr. Biol. 5:1995;747-757.
    • (1995) Curr. Biol. , vol.5 , pp. 747-757
    • Karin, M.1    Hunter, T.2
  • 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 Nat. Rev. Cancer. 2:2002;301-310.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.W.4
  • 23
    • 0034576494 scopus 로고    scopus 로고
    • The many substrates and functions of ATM
    • Kastan M.B., Lim D.S. The many substrates and functions of ATM. Nat. Rev. Mol. Cell Biol. 1:2000;179-186.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 179-186
    • Kastan, M.B.1    Lim, D.S.2
  • 25
    • 0037470238 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress
    • Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J., Durham T.L., Sung D.Y., Vierstra R.D. The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J. Biol. Chem. 278:2003;6862-6872.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6862-6872
    • Kurepa, J.1    Walker, J.M.2    Smalle, J.3    Gosink, M.M.4    Davis, S.J.5    Durham, T.L.6    Sung, D.Y.7    Vierstra, R.D.8
  • 26
    • 0032573165 scopus 로고    scopus 로고
    • Ionizing radiation and short wavelength UV activate NF-κB through two distinct mechanisms
    • Li N., Karin M. Ionizing radiation and short wavelength UV activate NF-κB through two distinct mechanisms. Proc. Natl. Acad. Sci. USA. 95:1998;13012-13017.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13012-13017
    • Li, N.1    Karin, M.2
  • 27
    • 0036781052 scopus 로고    scopus 로고
    • NF-κB regulation in the immune system
    • Li Q., Verma I.M. NF-κB regulation in the immune system. Nat. Rev. Immunol. 2:2002;725-734.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 28
    • 0034682890 scopus 로고    scopus 로고
    • Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3
    • Li H., Kolluri S.K., Gu J., Dawson M.I., Cao X., Hobbs P.D., Lin B., Chen G., Lu J., Lin F.et al. Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3. Science. 289:2000;1159-1164.
    • (2000) Science , vol.289 , pp. 1159-1164
    • Li, H.1    Kolluri, S.K.2    Gu, J.3    Dawson, M.I.4    Cao, X.5    Hobbs, P.D.6    Lin, B.7    Chen, G.8    Lu, J.9    Lin, F.10
  • 30
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell. 88:1997;97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 31
    • 0033588242 scopus 로고    scopus 로고
    • Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade
    • Mahanty S.K., Wang Y., Farley F.W., Elion E.A. Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade. Cell. 98:1999;501-512.
    • (1999) Cell , vol.98 , pp. 501-512
    • Mahanty, S.K.1    Wang, Y.2    Farley, F.W.3    Elion, E.A.4
  • 32
    • 0036724051 scopus 로고    scopus 로고
    • The carboxyl-terminal region of IκB kinase gamma (IKKγ) is required for full IKK activation
    • Makris C., Roberts J.L., Karin M. The carboxyl-terminal region of IκB kinase gamma (IKKγ) is required for full IKK activation. Mol. Cell. Biol. 22:2002;6573-6581.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6573-6581
    • Makris, C.1    Roberts, J.L.2    Karin, M.3
  • 33
    • 0035976962 scopus 로고    scopus 로고
    • IκBβ, but not IκBα, functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both NF-κB nuclear localization sequences in resting cells
    • Malek S., Chen Y., Huxford T., Ghosh G. IκBβ, but not IκBα, functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both NF-κB nuclear localization sequences in resting cells. J. Biol. Chem. 276:2001;45225-45235.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45225-45235
    • Malek, S.1    Chen, Y.2    Huxford, T.3    Ghosh, G.4
  • 34
    • 0034635958 scopus 로고    scopus 로고
    • SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage
    • Mao Y., Sun M., Desai S.D., Liu L.F. SUMO-1 conjugation to topoisomerase I. a possible repair response to topoisomerase-mediated DNA damage Proc. Natl. Acad. Sci. USA. 97:2000;4046-4051.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4046-4051
    • Mao, Y.1    Sun, M.2    Desai, S.D.3    Liu, L.F.4
  • 35
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis M.J., Coutavas E., Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1996;1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 36
    • 0034284715 scopus 로고    scopus 로고
    • Selective inhibiton 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., Ghosh S. Selective inhibiton of NF-κB activation by a peptide that blocks the interaction of NEMO with the IκB kinase complex. Science. 289:2000;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
  • 37
    • 0031594708 scopus 로고    scopus 로고
    • Novel IκBα degradation process in WEHI231 murine immature B cells
    • Miyamoto S., Seufzer B., Shumway S. Novel IκBα degradation process in WEHI231 murine immature B cells. Mol. Cell. Biol. 18:1998;19-29.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 19-29
    • Miyamoto, S.1    Seufzer, B.2    Shumway, S.3
  • 38
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller S., Matunis M.J., Dejean A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:1998;61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 41
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 43
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez M.S., Dargemont C., Hay R.T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276:2001;12654-12659.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 44
    • 0036809115 scopus 로고    scopus 로고
    • SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization
    • Ross S., Best J.L., Zon L.I., Gill G. SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization. Mol. Cell. 10:2002;831-842.
    • (2002) Mol. Cell , vol.10 , pp. 831-842
    • Ross, S.1    Best, J.L.2    Zon, L.I.3    Gill, G.4
  • 45
    • 0037044836 scopus 로고    scopus 로고
    • SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling
    • Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C. SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling. J. Biol. Chem. 277:2002;42981-42986.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42981-42986
    • Rui, H.L.1    Fan, E.2    Zhou, H.M.3    Xu, Z.4    Zhang, Y.5    Lin, S.C.6
  • 46
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • Salghetti S.E., Caudy A.A., Chenoweth J.G., Tansey W.P. Regulation of transcriptional activation domain function by ubiquitin. Science. 293:2001;1651-1653.
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 48
    • 0034713270 scopus 로고    scopus 로고
    • Genomic rearrangement in NEMO impairs NF-κB activation and is a cause of incontinentia pigmenti. The International Incontinentia Pigmenti (IP) Consortium
    • Smahi A., Courtois G., Vabres P., Yamaoka S., Heuertz S., Munnich A., Israel A., Heiss N.S., Klauck S.M., Kioschis P.et al. Genomic rearrangement in NEMO impairs NF-κB activation and is a cause of incontinentia pigmenti. The International Incontinentia Pigmenti (IP) Consortium. Nature. 405:2000;466-472.
    • (2000) Nature , vol.405 , pp. 466-472
    • Smahi, A.1    Courtois, G.2    Vabres, P.3    Yamaoka, S.4    Heuertz, S.5    Munnich, A.6    Israel, A.7    Heiss, N.S.8    Klauck, S.M.9    Kioschis, P.10
  • 49
    • 0033596125 scopus 로고    scopus 로고
    • Persistent activation of NF-κB by the tax transforming protein of HTLV-1: Hijacking cellular IκB kinases
    • Sun S.C., Ballard D.W. Persistent activation of NF-κB by the tax transforming protein of HTLV-1. hijacking cellular IκB kinases Oncogene. 18:1999;6948-6958.
    • (1999) Oncogene , vol.18 , pp. 6948-6958
    • Sun, S.C.1    Ballard, D.W.2
  • 50
    • 0035896543 scopus 로고    scopus 로고
    • IκB family members function by different mechanisms
    • Tam W.F., Sen R. IκB family members function by different mechanisms. J. Biol. Chem. 276:2001;7701-7704.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7701-7704
    • Tam, W.F.1    Sen, R.2
  • 52
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
    • Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H., Ashworth A., Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members. Nature. 424:2003;793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 54
    • 0037208074 scopus 로고    scopus 로고
    • Induction of the NF-κB cascade by recruitment of the scaffold molecule NEMO to the T-cell receptor
    • Weil R., Schwamborn K., Alcover A., Bessia C., Di Bartolo V., Israel A. Induction of the NF-κB cascade by recruitment of the scaffold molecule NEMO to the T-cell receptor. Immunity. 18:2003;13-26.
    • (2003) Immunity , vol.18 , pp. 13-26
    • Weil, R.1    Schwamborn, K.2    Alcover, A.3    Bessia, C.4    Di Bartolo, V.5    Israel, A.6
  • 55
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKKα is critical for cytokine-induced gene expression
    • Yamamoto Y., Verma U.N., Prajapati S., Kwak Y.T., Gaynor R.B. Histone H3 phosphorylation by IKKα is critical for cytokine-induced gene expression. Nature. 423:2003;655-659.
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 56
    • 0034707047 scopus 로고    scopus 로고
    • The DNA damage response: Putting checkpoints in perspective
    • Zhou B.B., Elledge S.J. The DNA damage response. putting checkpoints in perspective Nature. 408:2000;433-439.
    • (2000) Nature , vol.408 , pp. 433-439
    • Zhou, B.B.1    Elledge, S.J.2


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