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Volumn 7, Issue 5, 2012, Pages

NF-κB repression by PIAS3 mediated ReLA SUMOylation

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LEPTOMYCIN B; MUTANT PROTEIN; PROTEIN INHIBITOR OF ACTIVATED STAT; PROTEIN INHIBITOR OF ACTIVATED STAT 3; SUMO PROTEIN; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; GUANOSINE 3',5' POLYPHOSPHATE SYNTHETASES; GUANOSINE 3',5'-POLYPHOSPHATE SYNTHETASES; LIGASE; LUCIFERASE; UNSATURATED FATTY ACID;

EID: 84861386847     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037636     Document Type: Article
Times cited : (55)

References (38)
  • 1
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Ghosh S, Karin M, (2002) Missing pieces in the NF-kappaB puzzle. Cell 109 Supplpp. S81-96.
    • (2002) Cell , Issue.109 SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 2
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor kappaB signaling
    • Hoffmann A, Baltimore D, (2006) Circuitry of nuclear factor kappaB signaling. Immunol Rev 210: 171-186.
    • (2006) Immunol Rev , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 3
    • 0028967819 scopus 로고
    • Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B
    • Arenzana-Seisdedos F, Thompson J, Rodriguez MS, Bachelerie F, Thomas D, et al. (1995) Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B. Mol Cell Biol 15: 2689-2696.
    • (1995) Mol Cell Biol , vol.15 , pp. 2689-2696
    • Arenzana-Seisdedos, F.1    Thompson, J.2    Rodriguez, M.S.3    Bachelerie, F.4    Thomas, D.5
  • 4
    • 0031057644 scopus 로고    scopus 로고
    • Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm
    • Arenzana-Seisdedos F, Turpin P, Rodriguez M, Thomas D, Hay RT, et al. (1997) Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm. J Cell Sci 110 (Pt 3): 369-378.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 3 , pp. 369-378
    • Arenzana-Seisdedos, F.1    Turpin, P.2    Rodriguez, M.3    Thomas, D.4    Hay, R.T.5
  • 5
    • 0037044575 scopus 로고    scopus 로고
    • The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation
    • Hoffmann A, Levchenko A, Scott ML, Baltimore D, (2002) The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation. Science 298: 1241-1245.
    • (2002) Science , vol.298 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 6
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • Wertz IE, O'Rourke KM, Zhou H, Eby M, Aravind L, et al. (2004) De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature 430: 694-699.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5
  • 7
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp TR, Nijman SM, Dirac AM, Bernards R, (2003) Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424: 797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 8
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A, Chable-Bessia C, Cantarella G, Israel A, Wallach D, et al. (2003) The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 424: 801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5
  • 9
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, et al. (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424: 793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5
  • 11
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro JM, Rodriguez MS, Hay RT, (1998) SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 2: 233-239.
    • (1998) Mol Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 12
    • 33748188499 scopus 로고    scopus 로고
    • PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress
    • Mabb AM, Wuerzberger-Davis SM, Miyamoto S, (2006) PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress. Nat Cell Biol 8: 986-993.
    • (2006) Nat Cell Biol , vol.8 , pp. 986-993
    • Mabb, A.M.1    Wuerzberger-Davis, S.M.2    Miyamoto, S.3
  • 13
    • 23444461182 scopus 로고    scopus 로고
    • Regulation of gene-activation pathways by PIAS proteins in the immune system
    • Shuai K, Liu B, (2005) Regulation of gene-activation pathways by PIAS proteins in the immune system. Nat Rev Immunol 5: 593-605.
    • (2005) Nat Rev Immunol , vol.5 , pp. 593-605
    • Shuai, K.1    Liu, B.2
  • 14
    • 12844275070 scopus 로고    scopus 로고
    • Negative regulation of NF-kappaB signaling by PIAS1
    • Liu B, Yang R, Wong KA, Getman C, Stein N, et al. (2005) Negative regulation of NF-kappaB signaling by PIAS1. Mol Cell Biol 25: 1113-1123.
    • (2005) Mol Cell Biol , vol.25 , pp. 1113-1123
    • Liu, B.1    Yang, R.2    Wong, K.A.3    Getman, C.4    Stein, N.5
  • 15
    • 2642520591 scopus 로고    scopus 로고
    • PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit
    • Jang HD, Yoon K, Shin YJ, Kim J, Lee SY, (2004) PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit. J Biol Chem 279: 24873-24880.
    • (2004) J Biol Chem , vol.279 , pp. 24873-24880
    • Jang, H.D.1    Yoon, K.2    Shin, Y.J.3    Kim, J.4    Lee, S.Y.5
  • 16
    • 77951093007 scopus 로고    scopus 로고
    • Regulation of the psoriatic chemokine CCL20 by E3 ligases Trim32 and Piasy in keratinocytes
    • Liu Y, Lagowski JP, Gao S, Raymond JH, White CR, et al. (2010) Regulation of the psoriatic chemokine CCL20 by E3 ligases Trim32 and Piasy in keratinocytes. J Invest Dermatol 130: 1384-1390.
    • (2010) J Invest Dermatol , vol.130 , pp. 1384-1390
    • Liu, Y.1    Lagowski, J.P.2    Gao, S.3    Raymond, J.H.4    White, C.R.5
  • 17
    • 69249203574 scopus 로고    scopus 로고
    • SUMO association with repressor complexes, emerging routes for transcriptional control
    • Garcia-Dominguez M, Reyes JC, (2009) SUMO association with repressor complexes, emerging routes for transcriptional control. Biochim Biophys Acta 1789: 451-459.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 451-459
    • Garcia-Dominguez, M.1    Reyes, J.C.2
  • 18
    • 33744544785 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein
    • Dorval V, Fraser PE, (2006) Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein. J Biol Chem 281: 9919-9924.
    • (2006) J Biol Chem , vol.281 , pp. 9919-9924
    • Dorval, V.1    Fraser, P.E.2
  • 19
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation
    • Mercurio F, Zhu H, Murray BW, Shevchenko A, Bennett BL, et al. (1997) IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation. Science 278: 860-866.
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.1    Zhu, H.2    Murray, B.W.3    Shevchenko, A.4    Bennett, B.L.5
  • 20
    • 0027436552 scopus 로고
    • 7,12-Dimethylbenz[a]anthracene-induced mouse keratinocyte malignant transformation independent of Harvey ras activation
    • Schneider BL, Bowden GT, Sutter C, Schweizer J, Han KA, et al. (1993) 7,12-Dimethylbenz[a]anthracene-induced mouse keratinocyte malignant transformation independent of Harvey ras activation. JInvest Dermatol 101: 595.
    • (1993) JInvest Dermatol , vol.101 , pp. 595
    • Schneider, B.L.1    Bowden, G.T.2    Sutter, C.3    Schweizer, J.4    Han, K.A.5
  • 21
    • 36349030782 scopus 로고    scopus 로고
    • Microtubule disruption and tumor suppression by mitogen-activated protein kinase phosphatase 4
    • Liu Y, Lagowski J, Sundholm A, Sundberg A, Kulesz-Martin M, (2007) Microtubule disruption and tumor suppression by mitogen-activated protein kinase phosphatase 4. Cancer Res 67: 10711-10719.
    • (2007) Cancer Res , vol.67 , pp. 10711-10719
    • Liu, Y.1    Lagowski, J.2    Sundholm, A.3    Sundberg, A.4    Kulesz-Martin, M.5
  • 22
    • 0035878718 scopus 로고    scopus 로고
    • Functional quantification of DNA-binding proteins p53 and estrogen receptor in cells and tumor tissues by DNA affinity immunoblotting
    • Liu Y, Asch H, Kulesz-Martin MF, (2001) Functional quantification of DNA-binding proteins p53 and estrogen receptor in cells and tumor tissues by DNA affinity immunoblotting. Cancer Res 61: 5402.
    • (2001) Cancer Res , vol.61 , pp. 5402
    • Liu, Y.1    Asch, H.2    Kulesz-Martin, M.F.3
  • 23
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez MS, Dargemont C, Hay RT, (2001) SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem 276: 12654-12659.
    • (2001) J Biol Chem , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 24
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: a history of modification
    • Hay RT, (2005) SUMO: a history of modification. Mol Cell 18: 1-12.
    • (2005) Mol Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 25
    • 0030824331 scopus 로고    scopus 로고
    • Distinct domains of the RelA NF-kappaB subunit are required for negative cross-talk and direct interaction with the glucocorticoid receptor
    • Wissink S, van Heerde EC, Schmitz ML, Kalkhoven E, van der Burg B, et al. (1997) Distinct domains of the RelA NF-kappaB subunit are required for negative cross-talk and direct interaction with the glucocorticoid receptor. J Biol Chem 272: 22278-22284.
    • (1997) J Biol Chem , vol.272 , pp. 22278-22284
    • Wissink, S.1    van Heerde, E.C.2    Schmitz, M.L.3    Kalkhoven, E.4    van der Burg, B.5
  • 26
    • 34247348215 scopus 로고    scopus 로고
    • Opposing LSD1 complexes function in developmental gene activation and repression programmes
    • Wang J, Scully K, Zhu X, Cai L, Zhang J, et al. (2007) Opposing LSD1 complexes function in developmental gene activation and repression programmes. Nature 446: 882-887.
    • (2007) Nature , vol.446 , pp. 882-887
    • Wang, J.1    Scully, K.2    Zhu, X.3    Cai, L.4    Zhang, J.5
  • 27
    • 0033859780 scopus 로고    scopus 로고
    • A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy
    • Iniguez-Lluhi JA, Pearce D, (2000) A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy. Mol Cell Biol 20: 6040-6050.
    • (2000) Mol Cell Biol , vol.20 , pp. 6040-6050
    • Iniguez-Lluhi, J.A.1    Pearce, D.2
  • 28
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, et al. (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol Cell 39: 641-652.
    • (2010) Mol Cell , vol.39 , pp. 641-652
    • Matic, I.1    Schimmel, J.2    Hendriks, I.A.3    van Santen, M.A.4    van de Rijke, F.5
  • 29
    • 24944528328 scopus 로고    scopus 로고
    • SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast
    • Shin JA, Choi ES, Kim HS, Ho JC, Watts FZ, et al. (2005) SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast. Mol Cell 19: 817-828.
    • (2005) Mol Cell , vol.19 , pp. 817-828
    • Shin, J.A.1    Choi, E.S.2    Kim, H.S.3    Ho, J.C.4    Watts, F.Z.5
  • 30
    • 0034993496 scopus 로고    scopus 로고
    • The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family
    • Hari KL, Cook KR, Karpen GH, (2001) The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family. Genes Dev 15: 1334-1348.
    • (2001) Genes Dev , vol.15 , pp. 1334-1348
    • Hari, K.L.1    Cook, K.R.2    Karpen, G.H.3
  • 31
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • David G, Neptune MA, DePinho RA, (2002) SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J Biol Chem 277: 23658-23663.
    • (2002) J Biol Chem , vol.277 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    DePinho, R.A.3
  • 32
    • 0038054467 scopus 로고    scopus 로고
    • Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding
    • Lin X, Sun B, Liang M, Liang YY, Gast A, et al. (2003) Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding. Mol Cell 11: 1389-1396.
    • (2003) Mol Cell , vol.11 , pp. 1389-1396
    • Lin, X.1    Sun, B.2    Liang, M.3    Liang, Y.Y.4    Gast, A.5
  • 33
    • 64749093273 scopus 로고    scopus 로고
    • Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex
    • Ouyang J, Shi Y, Valin A, Xuan Y, Gill G, (2009) Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol Cell 34: 145-154.
    • (2009) Mol Cell , vol.34 , pp. 145-154
    • Ouyang, J.1    Shi, Y.2    Valin, A.3    Xuan, Y.4    Gill, G.5
  • 34
    • 77958173509 scopus 로고    scopus 로고
    • The ligase PIAS1 restricts natural regulatory T cell differentiation by epigenetic repression
    • Liu B, Tahk S, Yee KM, Fan G, Shuai K, (2010) The ligase PIAS1 restricts natural regulatory T cell differentiation by epigenetic repression. Science 330: 521-525.
    • (2010) Science , vol.330 , pp. 521-525
    • Liu, B.1    Tahk, S.2    Yee, K.M.3    Fan, G.4    Shuai, K.5
  • 35
    • 55549140173 scopus 로고    scopus 로고
    • Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation
    • Li Y, Reddy MA, Miao F, Shanmugam N, Yee JK, et al. (2008) Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation. J Biol Chem 283: 26771-26781.
    • (2008) J Biol Chem , vol.283 , pp. 26771-26781
    • Li, Y.1    Reddy, M.A.2    Miao, F.3    Shanmugam, N.4    Yee, J.K.5
  • 36
    • 0037462725 scopus 로고    scopus 로고
    • Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65
    • Kiernan R, Bres V, Ng RW, Coudart MP, El Messaoudi S, et al. (2003) Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65. J Biol Chem 278: 2758-2766.
    • (2003) J Biol Chem , vol.278 , pp. 2758-2766
    • Kiernan, R.1    Bres, V.2    Ng, R.W.3    Coudart, M.P.4    El Messaoudi, S.5
  • 37
    • 48749085156 scopus 로고    scopus 로고
    • Encoding NF-kappaB temporal control in response to TNF: distinct roles for the negative regulators IkappaBalpha and A20
    • Werner SL, Kearns JD, Zadorozhnaya V, Lynch C, O'Dea E, et al. (2008) Encoding NF-kappaB temporal control in response to TNF: distinct roles for the negative regulators IkappaBalpha and A20. Genes Dev 22: 2093-2101.
    • (2008) Genes Dev , vol.22 , pp. 2093-2101
    • Werner, S.L.1    Kearns, J.D.2    Zadorozhnaya, V.3    Lynch, C.4    O'Dea, E.5
  • 38
    • 0025304791 scopus 로고
    • Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA
    • Zabel U, Baeuerle PA, (1990) Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA. Cell 61: 255-265.
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2


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