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Volumn 13, Issue 2, 2003, Pages 108-113

Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HEAT SHOCK TRANSCRIPTION FACTOR 1; ISOPROTEIN; LYSINE; OXYGENASE; SUMO 1 PROTEIN; SUMO PROTEIN; TRANSCRIPTION FACTOR SP3;

EID: 0037382641     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(03)00021-2     Document Type: Review
Times cited : (199)

References (48)
  • 6
    • 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. • Endogenous Sp3 is shown to be post-translationally modified by SUMO-1 and the major SUMO acceptor site is mapped to a previously defined inhibitory domain. Removal of SUMO-1 from Sp3 by mutation of the acceptor lysines or cotransfection with the SuPr-1 SUMO protease increased transcriptional activation by Sp3. SUMO-1 modification was also shown to regulate the subnuclear localization of Sp3 to the nuclear periphery and nuclear dots. The authors show that covalent attachment of SUMO-1 by gene fusion is sufficient to regulate Sp3 activity and localization.
    • (2002) Mol. Cell , vol.10 , pp. 831-842
    • Ross, S.1    Best, J.L.2    Zon, L.I.3    Gill, G.4
  • 7
    • 0036792683 scopus 로고    scopus 로고
    • Transcription factor Sp3 is silenced through SUMO modification by PIAS1
    • ••] the transcription factor Sp3 is shown to be post-translationally modified by SUMO-1 at a lysine residue in a known inhibitory domain. PIAS1 is shown to interact with Sp3 and stimulate SUMO-modification of Sp3 in vitro. Mutations in Sp3 that prevent SUMO modification in vitro greatly enhance transcriptional activation by Sp3 in vivo. SUMO modification does not alter Sp3 DNA binding activity in vitro.
    • (2002) EMBO J. , vol.21 , pp. 5206-5215
    • Sapetschnig, A.1    Rischitor, G.2    Braun, H.3    Doll, A.4    Schergaut, M.5    Melchior, F.6    Suske, G.7
  • 8
    • 0036721526 scopus 로고    scopus 로고
    • Potentiation of glucocorticoid receptor transcriptional activity by sumoylation
    • Le Drean Y., Mincheneau N., Le Goff P., Michel D. Potentiation of glucocorticoid receptor transcriptional activity by sumoylation. Endocrinology. 143:2002;3482-3489. • GR is shown to be post-translationally modified by SUMO-1. Overexpression of SUMO-1 was found to stimulate GR-dependent transcription in a promoter-specific manner. In particular, overexpression of SUMO-1 stimulated GR activation from multiple but not single binding sites, suggesting SUMO-1 may regulate synergistic activation by GR.
    • (2002) Endocrinology , vol.143 , pp. 3482-3489
    • Le Drean, Y.1    Mincheneau, N.2    Le Goff, P.3    Michel, D.4
  • 9
    • 0036847208 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor
    • •], mutating the SUMO acceptor lysines was found to increase GR activity at some promoters but not others, suggesting promoter-specific effects of this post-translational modification.
    • (2002) Biochem. J. , vol.367 , pp. 907-911
    • Tian, S.1    Poukka, H.2    Palvimo, J.J.3    Janne, O.A.4
  • 11
    • 0036237383 scopus 로고    scopus 로고
    • Versatile protein tag, SUMO: Its enzymology and biological function
    • Kim K.I., Baek S.H., Chung C.H. Versatile protein tag, SUMO: its enzymology and biological function. J. Cell Physiol. 191:2002;257-268.
    • (2002) J. Cell Physiol. , vol.191 , pp. 257-268
    • Kim, K.I.1    Baek, S.H.2    Chung, C.H.3
  • 12
    • 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
  • 14
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo T., Nishida T., Yasuda H. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell. 8:2001;713-718. • Although the SUMO E1 activating enzyme and E2 conjugating enzyme are sufficient for a low level of sumoylation in vitro, this study shows that PIAS1 acts as a SUMO E3 ligase to stimulate SUMO-modification of the tumor suppressor p53 in vitro and in vivo. Consistent with its role as a SUMO E3 ligase, PIAS1 is shown to interact with both the Ubc 9 E2 conjugating enzyme and the substrate p53. SUMO E3 ligase activity of PIAS1 is dependent on an intact RING domain.
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 15
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • Sachdev S., Bruhn L., Sieber H., Pichler A., Melchior F., Grosschedl R. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev. 15:2001;3088-3103. • This study identifies PIASy as a SUMO E3 ligase for the Wnt-responsive transcription factor LEF1. PIASy is shown to stimulate SUMO-modification of LEF1 both in vitro and in vivo dependent on the RING domain of PIASy. PIASy represses LEF1-dependent transcription and regulates LEF1 subnuclear localization into nuclear bodies. Regulation of LEF1 activity and localization depends on the RING domain of PIASy but not the major SUMO acceptor sites in LEF1, suggesting that although PIASy E3 ligase activity is required, LEF1 may not be the critical substrate for these functional effects.
    • (2001) Genes Dev. , vol.15 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 16
    • 0037059619 scopus 로고    scopus 로고
    • The Nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler A., Gast A., Seeler J.S., Dejean A., Melchior F. The Nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell. 108:2002;109-120. • This paper identifies the nucleoporin component RanBP2 as a SUMO E3 ligase. RanBP2 stimulates SUMO modification of RanGAP but not p53 in vitro. RanBP2 does not have a RING domain and shows no homology to the PIAS family of SUMO E3 ligases.
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 18
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K. Specific inhibition of Stat3 signal transduction by PIAS3. Science. 278:1997;1803-1805.
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1    Liao, J.2    Liu, B.3    Rao, X.4    Jay, P.5    Berta, P.6    Shuai, K.7
  • 19
    • 0034530046 scopus 로고    scopus 로고
    • ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation
    • Kotaja N., Aittomaki S., Silvennoinen O., Palvimo J.J., Janne O.A. ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation. Mol. Endocrinol. 14:2000;1986-2000.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1986-2000
    • Kotaja, N.1    Aittomaki, S.2    Silvennoinen, O.3    Palvimo, J.J.4    Janne, O.A.5
  • 20
    • 0035963311 scopus 로고    scopus 로고
    • Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells
    • Gross M., Liu B., Tan J., French F.S., Carey M., Shuai K. Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells. Oncogene. 20:2001;3880-3887.
    • (2001) Oncogene , vol.20 , pp. 3880-3887
    • Gross, M.1    Liu, B.2    Tan, J.3    French, F.S.4    Carey, M.5    Shuai, K.6
  • 21
    • 0037041024 scopus 로고    scopus 로고
    • Activation of p53 by protein inhibitor of activated Stat1 (PIAS1)
    • Megidish T., Xu J.H., Xu C.W. Activation of p53 by protein inhibitor of activated Stat1 (PIAS1). J. Biol. Chem. 277:2002;8255-8259.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8255-8259
    • Megidish, T.1    Xu, J.H.2    Xu, C.W.3
  • 22
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin- specific protease
    • Gong L., Millas S., Maul G.G., Yeh E.T. Differential regulation of sentrinized proteins by a novel sentrin- specific protease. J. Biol. Chem. 275:2000;3355-3359.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 23
    • 0033760171 scopus 로고    scopus 로고
    • A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase
    • Nishida T., Tanaka H., Yasuda H. A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. Eur. J. Biochem. 267:2000;6423-6427.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6423-6427
    • Nishida, T.1    Tanaka, H.2    Yasuda, H.3
  • 24
    • 0035914357 scopus 로고    scopus 로고
    • Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation
    • Nishida T., Kaneko F., Kitagawa M., Yasuda H. Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation. J. Biol. Chem. 276:2001;39060-39066.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39060-39066
    • Nishida, T.1    Kaneko, F.2    Kitagawa, M.3    Yasuda, H.4
  • 25
    • 0037205460 scopus 로고    scopus 로고
    • Association of the human SUMO-1 protease SENP2 with the nuclear pore
    • Hang J., Dasso M. Association of the human SUMO-1 protease SENP2 with the nuclear pore. J. Biol. Chem. 277:2002;19961-19966.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 26
    • 0036809116 scopus 로고    scopus 로고
    • SUMO-1 Protease-1 (SuPr-1) regulates gene transcription through PML
    • Best J.L., Ganiatsas S., Agarwal S., Changou A., Salomoni P., Shirihai O., Meluh P.B., Pandolfi P.P., Zon L.I. SUMO-1 Protease-1 (SuPr-1) regulates gene transcription through PML. Mol. Cell. 10:2002;843-855. • The authors identify the SUMO protease SuPr-1 as an activator of c-jun dependent transcription. SuPr-1 localizes to PML nuclear bodies and removes SUMO-1 from PML but not RanGAP1 in vivo. Binding of wild-type or a catalytically inactive mutant of SuPr-1 to SUMO-modified PML alters localization of several proteins found in PML nuclear bodies including PML and CBP. This study shows that SUMO proteases may regulate transcription factor activity by multiple mechanisms.
    • (2002) Mol. Cell , vol.10 , pp. 843-855
    • Best, J.L.1    Ganiatsas, S.2    Agarwal, S.3    Changou, A.4    Salomoni, P.5    Shirihai, O.6    Meluh, P.B.7    Pandolfi, P.P.8    Zon, L.I.9
  • 27
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • Bies J., Markus J., Wolff L. Covalent attachment of SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J. Biol. Chem. 277:2002;8999-9009.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 28
    • 0037064083 scopus 로고    scopus 로고
    • Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation
    • Kim J., Cantwell C.A., Johnson P.F., Pfarr C.M., Williams S.C. Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation. J. Biol. Chem. 277:2002;38037-38044. • In this study, the authors show that a previously identified inhibitory domain in C/EBP is a site of SUMO-modification. This domain inhibits transcriptional activation in a copy-number-dependent manner, both in cis and in trans, dependent on the integrity of the consensus SUMO acceptor site.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38037-38044
    • Kim, J.1    Cantwell, C.A.2    Johnson, P.F.3    Pfarr, C.M.4    Williams, S.C.5
  • 29
    • 0029902383 scopus 로고    scopus 로고
    • An inhibitor domain in Sp3 regulates its glutamine-rich activation domains
    • Dennig J., Beato M., Suske G. An inhibitor domain in Sp3 regulates its glutamine-rich activation domains. EMBO J. 15:1996;5659-5667.
    • (1996) EMBO J. , vol.15 , pp. 5659-5667
    • Dennig, J.1    Beato, M.2    Suske, G.3
  • 30
    • 0033859780 scopus 로고    scopus 로고
    • A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy
    • Iniguez-Lluhi J.A., Pearce D. A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy. Mol. Cell Biol. 20:2000;6040-6050.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6040-6050
    • Iniguez-Lluhi, J.A.1    Pearce, D.2
  • 31
    • 0035955662 scopus 로고    scopus 로고
    • Regulation of heat shock transcription factor 1 by stress-induced SUMO- 1 modification
    • Hong Y., Rogers R., Matunis M.J., Mayhew C.N., Goodson M.L., Park-Sarge O.K., Sarge K.D., Goodson M. Regulation of heat shock transcription factor 1 by stress-induced SUMO- 1 modification. J. Biol. Chem. 276:2001;40263-40267. • In this paper, the authors show that heat shock transcription factor 1, HSF1, is post-translationally modified by SUMO-1 upon exposure to elevated temperatures. SUMO-1 modification is shown to stimulate DNA binding by HSF1 in vitro. Upon heat shock, wild-type HSF, but not a mutant in the SUMO acceptor lysine, is localized to nuclear bodies.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40263-40267
    • Hong, Y.1    Rogers, R.2    Matunis, M.J.3    Mayhew, C.N.4    Goodson, M.L.5    Park-Sarge, O.K.6    Sarge, K.D.7    Goodson, M.8
  • 33
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner M., Jenuwein T. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14:2002;286-298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 34
    • 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
  • 36
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • Mahajan R., Gerace L., Melchior F. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140:1998;259-270.
    • (1998) J. Cell Biol. , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 37
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
    • Matunis M.J., Wu J., Blobel G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140:1998;499-509.
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 38
    • 0034700082 scopus 로고    scopus 로고
    • Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell- cycle-dependent assembly into nuclear bodies
    • Chakrabarti S.R., Sood R., Nandi S., Nucifora G. Posttranslational modification of TEL and TEL/AML1 by SUMO-1 and cell- cycle-dependent assembly into nuclear bodies. Proc. Natl. Acad. Sci. U.S.A. 97:2000;13281-13285.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13281-13285
    • Chakrabarti, S.R.1    Sood, R.2    Nandi, S.3    Nucifora, G.4
  • 41
    • 0036066181 scopus 로고    scopus 로고
    • Modification of Daxx by small ubiquitin-related modifier-1
    • Jang M.S., Ryu S.W., Kim E. Modification of Daxx by small ubiquitin-related modifier-1. Biochem. Biophys. Res. Commun. 295:2002;495-500.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 495-500
    • Jang, M.S.1    Ryu, S.W.2    Kim, E.3
  • 42
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf T., Jensen K., Reich B., Will H. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274:1999;12555-12566.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 43
    • 0035969102 scopus 로고    scopus 로고
    • SUMO: Of branched proteins and nuclear bodies
    • Seeler J.S., Dejean A. SUMO: of branched proteins and nuclear bodies. Oncogene. 20:2001;7243-7249.
    • (2001) Oncogene , vol.20 , pp. 7243-7249
    • Seeler, J.S.1    Dejean, A.2
  • 44
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong S., Salomoni P., Pandolfi P.P. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2:2000;E85-E90.
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 45
    • 0032498230 scopus 로고    scopus 로고
    • The enhanceosome and transcriptional synergy
    • Carey M. The enhanceosome and transcriptional synergy. Cell. 92:1998;5-8.
    • (1998) Cell , vol.92 , pp. 5-8
    • Carey, M.1
  • 46
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H., Karvonen U., Janne O.A., Palvimo J.J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U.S.A. 97:2000;14145-14150.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 47
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway R.C., Brower C.S., Conaway J.W. Emerging roles of ubiquitin in transcription regulation. Science. 296:2002;1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 48
    • 0036348150 scopus 로고    scopus 로고
    • Dual regulation of the met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment
    • Kuras L., Rouillon A., Lee T., Barbey R., Tyers M., Thomas D. Dual regulation of the met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment. Mol. Cell. 10:2002;69-80. • Met4 activates expression of the MET genes in yeast when methionine is limiting. In minimal media supplemented with methionine, ubiquitination of Met4 leads to proteasome-dependent degradation. In this paper, the authors show that in rich media Met4 is modified by ubiquitin but remains stable. Under these conditions, ubiquitinated Met4 is not recruited to the MET promoters but is recruited to the SAM genes. The results suggest a role for post-translational modification by ubiquitin in promoter-specific regulation of transcription.
    • (2002) Mol. Cell , vol.10 , pp. 69-80
    • Kuras, L.1    Rouillon, A.2    Lee, T.3    Barbey, R.4    Tyers, M.5    Thomas, D.6


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