메뉴 건너뛰기




Volumn 1812, Issue 8, 2011, Pages 909-918

Transcriptional control of metabolic and inflammatory pathways by nuclear receptor SUMOylation

Author keywords

Acute phase response; GPS2; Inflammation; LRH 1; LXR; Metabolism; N CoR; Nuclear receptor; Post translational modification; PPAR; SMRT; SUMO; Transrepression

Indexed keywords

ANTIINFLAMMATORY AGENT; BIOTIN; CELL NUCLEUS RECEPTOR; CHOLESTEROL 7ALPHA MONOOXYGENASE; COENZYME A; DAXX PROTEIN; HISTONE DEACETYLASE 4; LIVER RECEPTOR HOMOLOG 1; LIVER X RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN INHIBITOR OF ACTIVATED STAT; PROTEIN UBC9; REACTIVE OXYGEN METABOLITE; RETINOID X RECEPTOR; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; TRANSCRIPTION FACTOR AP 1;

EID: 79958244237     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2010.12.008     Document Type: Review
Times cited : (75)

References (134)
  • 1
    • 33747816546 scopus 로고    scopus 로고
    • Lives and times of nuclear receptors
    • Alarid E.T. Lives and times of nuclear receptors. Mol. Endocrinol. 2006, 20:1972-1981.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1972-1981
    • Alarid, E.T.1
  • 2
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling
    • Reid G., Hubner M.R., Metivier R., Brand H., Denger S., Manu D., Beaudouin J., Ellenberg J., Gannon F. Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 2003, 11:695-707.
    • (2003) Mol. Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 3
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M. Origin and function of ubiquitin-like proteins. Nature 2009, 458:422-429.
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 4
    • 33646009148 scopus 로고    scopus 로고
    • Role of ubiquitin-like proteins in transcriptional regulation
    • Hay R.T. Role of ubiquitin-like proteins in transcriptional regulation. Ernst Schering Res. Found. Workshop 2006, 173-192.
    • (2006) Ernst Schering Res. Found. Workshop , pp. 173-192
    • Hay, R.T.1
  • 5
    • 34248338373 scopus 로고    scopus 로고
    • SUMO: regulating the regulator
    • Bossis G., Melchior F. SUMO: regulating the regulator. Cell Div. 2006, 1:13.
    • (2006) Cell Div. , vol.1 , pp. 13
    • Bossis, G.1    Melchior, F.2
  • 7
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: a history of modification
    • Hay R.T. SUMO: a history of modification. Mol. Cell 2005, 18:1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 8
    • 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 1997, 88:97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 9
    • 37749037140 scopus 로고    scopus 로고
    • PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription
    • Palvimo J.J. PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription. Biochem. Soc. Trans. 2007, 35:1405-1408.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1405-1408
    • Palvimo, J.J.1
  • 10
    • 33845970925 scopus 로고    scopus 로고
    • Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma
    • Ghisletti S., Huang W., Ogawa S., Pascual G., Lin M.E., Willson T.M., Rosenfeld M.G., Glass C.K. Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma. Mol. Cell 2007, 25:57-70.
    • (2007) Mol. Cell , vol.25 , pp. 57-70
    • Ghisletti, S.1    Huang, W.2    Ogawa, S.3    Pascual, G.4    Lin, M.E.5    Willson, T.M.6    Rosenfeld, M.G.7    Glass, C.K.8
  • 11
    • 77953318097 scopus 로고    scopus 로고
    • HDAC2 promotes eIF4E sumoylation and activates mRNA translation gene specifically
    • Xu X., Vatsyayan J., Gao C., Bakkenist C.J., Hu J. HDAC2 promotes eIF4E sumoylation and activates mRNA translation gene specifically. J. Biol. Chem. 2010, 285:18139-18143.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18139-18143
    • Xu, X.1    Vatsyayan, J.2    Gao, C.3    Bakkenist, C.J.4    Hu, J.5
  • 12
    • 14844344773 scopus 로고    scopus 로고
    • Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors
    • Gregoire S., Yang X.J. Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors. Mol. Cell. Biol. 2005, 25:2273-2287.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2273-2287
    • Gregoire, S.1    Yang, X.J.2
  • 13
    • 33846216376 scopus 로고    scopus 로고
    • Wrestling rules in transrepression: as easy as SUMO-1, -2, -3-
    • Treuter E., Gustafsson J.A. Wrestling rules in transrepression: as easy as SUMO-1, -2, -3- Mol. Cell 2007, 25:178-180.
    • (2007) Mol. Cell , vol.25 , pp. 178-180
    • Treuter, E.1    Gustafsson, J.A.2
  • 15
    • 77950643586 scopus 로고    scopus 로고
    • The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif
    • Yang S.H., Sharrocks A.D. The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif. Mol. Cell. Biol. 2010, 30:2193-2205.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2193-2205
    • Yang, S.H.1    Sharrocks, A.D.2
  • 17
    • 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 2002, 108:109-120.
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 18
    • 79958281723 scopus 로고    scopus 로고
    • SUMO E3 ligase activity of TRIM proteins
    • Oct 25. [Electronic publication ahead of print]
    • Chu Y., Yang X. SUMO E3 ligase activity of TRIM proteins. Oncogene 2010, Oct 25. [Electronic publication ahead of print].
    • (2010) Oncogene
    • Chu, Y.1    Yang, X.2
  • 19
    • 34548483908 scopus 로고    scopus 로고
    • SUMO-specific proteases: a twist in the tail
    • Hay R.T. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 2007, 17:370-376.
    • (2007) Trends Cell Biol. , vol.17 , pp. 370-376
    • Hay, R.T.1
  • 20
    • 33748416853 scopus 로고    scopus 로고
    • A recurrent phospho-sumoyl switch in transcriptional repression and beyond
    • Yang X.J., Gregoire S. A recurrent phospho-sumoyl switch in transcriptional repression and beyond. Mol. Cell 2006, 23:779-786.
    • (2006) Mol. Cell , vol.23 , pp. 779-786
    • Yang, X.J.1    Gregoire, S.2
  • 23
    • 40849126935 scopus 로고    scopus 로고
    • Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif
    • Tremblay A.M., Wilson B.J., Yang X.J., Giguere V. Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif. Mol. Endocrinol. 2008, 22:570-584.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 570-584
    • Tremblay, A.M.1    Wilson, B.J.2    Yang, X.J.3    Giguere, V.4
  • 25
    • 25844437172 scopus 로고    scopus 로고
    • Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest
    • Ulrich H.D. Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest. Trends Cell Biol. 2005, 15:525-532.
    • (2005) Trends Cell Biol. , vol.15 , pp. 525-532
    • Ulrich, H.D.1
  • 26
    • 65649101212 scopus 로고    scopus 로고
    • Crosstalk between sumoylation and acetylation regulates p53-dependent chromatin transcription and DNA binding
    • Wu S.Y., Chiang C.M. Crosstalk between sumoylation and acetylation regulates p53-dependent chromatin transcription and DNA binding. EMBO J. 2009, 28:1246-1259.
    • (2009) EMBO J. , vol.28 , pp. 1246-1259
    • Wu, S.Y.1    Chiang, C.M.2
  • 27
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress
    • Huang T.T., Wuerzberger-Davis S.M., Wu Z.H., Miyamoto S. Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell 2003, 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
  • 28
    • 70350443607 scopus 로고    scopus 로고
    • Proteomic revelation: SUMO changes partners when the heat is on
    • Flick K., Kaiser P. Proteomic revelation: SUMO changes partners when the heat is on. Sci. Signal. 2009, 2:e45.
    • (2009) Sci. Signal. , vol.2
    • Flick, K.1    Kaiser, P.2
  • 29
    • 63549136610 scopus 로고    scopus 로고
    • Sumoylation and human disease pathogenesis
    • Sarge K.D., Park-Sarge O.K. Sumoylation and human disease pathogenesis. Trends Biochem. Sci. 2009, 34:200-205.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 200-205
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 30
    • 77956226226 scopus 로고    scopus 로고
    • Emerging roles of SUMO modification in arthritis
    • Yan D., Davis F.J., Sharrocks A.D., Im H.J. Emerging roles of SUMO modification in arthritis. Gene 2010, 466:1-15.
    • (2010) Gene , vol.466 , pp. 1-15
    • Yan, D.1    Davis, F.J.2    Sharrocks, A.D.3    Im, H.J.4
  • 31
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • Rosenfeld M.G., Lunyak V.V., Glass C.K. Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 2006, 20:1405-1428.
    • (2006) Genes Dev. , vol.20 , pp. 1405-1428
    • Rosenfeld, M.G.1    Lunyak, V.V.2    Glass, C.K.3
  • 32
    • 33644636344 scopus 로고    scopus 로고
    • Going nuclear in metabolic and cardiovascular disease
    • Glass C.K. Going nuclear in metabolic and cardiovascular disease. J. Clin. Investig. 2006, 116:556-560.
    • (2006) J. Clin. Investig. , vol.116 , pp. 556-560
    • Glass, C.K.1
  • 33
    • 77951602823 scopus 로고    scopus 로고
    • Nuclear receptor transrepression pathways that regulate inflammation in macrophages and T cells
    • Glass C.K., Saijo K. Nuclear receptor transrepression pathways that regulate inflammation in macrophages and T cells. Nat. Rev. Immunol. 2010, 10:365-376.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 365-376
    • Glass, C.K.1    Saijo, K.2
  • 34
    • 77955170550 scopus 로고    scopus 로고
    • Nuclear receptors and inflammation control: molecular mechanisms and pathophysiological relevance
    • Huang W., Glass C.K. Nuclear receptors and inflammation control: molecular mechanisms and pathophysiological relevance. Arterioscler. Thromb. Vasc. Biol. 2010, 30:1542-1549.
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 1542-1549
    • Huang, W.1    Glass, C.K.2
  • 35
    • 33244482536 scopus 로고    scopus 로고
    • Combinatorial roles of nuclear receptors in inflammation and immunity
    • Glass C.K., Ogawa S. Combinatorial roles of nuclear receptors in inflammation and immunity. Nat. Rev. 2006, 6:44-55.
    • (2006) Nat. Rev. , vol.6 , pp. 44-55
    • Glass, C.K.1    Ogawa, S.2
  • 38
    • 75649135910 scopus 로고    scopus 로고
    • Deconstructing repression: evolving models of co-repressor action
    • Perissi V., Jepsen K., Glass C.K., Rosenfeld M.G. Deconstructing repression: evolving models of co-repressor action. Nat. Rev. Genet. 2010, 11:109-123.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 109-123
    • Perissi, V.1    Jepsen, K.2    Glass, C.K.3    Rosenfeld, M.G.4
  • 39
    • 27844509037 scopus 로고    scopus 로고
    • Transcriptional corepression by SHP: molecular mechanisms and physiological consequences
    • Bavner A., Sanyal S., Gustafsson J.A., Treuter E. Transcriptional corepression by SHP: molecular mechanisms and physiological consequences. Trends Endocrinol. Metab. 2005, 16:478-488.
    • (2005) Trends Endocrinol. Metab. , vol.16 , pp. 478-488
    • Bavner, A.1    Sanyal, S.2    Gustafsson, J.A.3    Treuter, E.4
  • 40
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • Lin J., Handschin C., Spiegelman B.M. Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab. 2005, 1:361-370.
    • (2005) Cell Metab. , vol.1 , pp. 361-370
    • Lin, J.1    Handschin, C.2    Spiegelman, B.M.3
  • 41
    • 73349085238 scopus 로고    scopus 로고
    • Steroid receptor phosphorylation: assigning function to site-specific phosphorylation
    • Ward R.D., Weigel N.L. Steroid receptor phosphorylation: assigning function to site-specific phosphorylation. Biofactors 2009, 35:528-536.
    • (2009) Biofactors , vol.35 , pp. 528-536
    • Ward, R.D.1    Weigel, N.L.2
  • 42
    • 77952135293 scopus 로고    scopus 로고
    • Mechanisms of resistance to hormonal treatment in breast cancer
    • Eroles P., Bosch A., Bermejo B., Lluch A. Mechanisms of resistance to hormonal treatment in breast cancer. Clin. Transl. Oncol. 2010, 12:246-252.
    • (2010) Clin. Transl. Oncol. , vol.12 , pp. 246-252
    • Eroles, P.1    Bosch, A.2    Bermejo, B.3    Lluch, A.4
  • 45
    • 69449102498 scopus 로고    scopus 로고
    • Minireview: role of protein methylation and demethylation in nuclear hormone signaling
    • Wu S.C., Zhang Y. Minireview: role of protein methylation and demethylation in nuclear hormone signaling. Mol. Endocrinol. 2009, 23:1323-1334.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 1323-1334
    • Wu, S.C.1    Zhang, Y.2
  • 47
    • 34249796386 scopus 로고    scopus 로고
    • Ubiquitin-like protein modifications in prostate and breast cancer
    • Wu F., Mo Y.Y. Ubiquitin-like protein modifications in prostate and breast cancer. Front. Biosci. 2007, 12:700-711.
    • (2007) Front. Biosci. , vol.12 , pp. 700-711
    • Wu, F.1    Mo, Y.Y.2
  • 48
    • 76449110896 scopus 로고    scopus 로고
    • SUMO and ubiquitin modifications during steroid hormone synthesis and function
    • Talamillo A., Martin D., Hjerpe R., Sanchez J., Barrio R. SUMO and ubiquitin modifications during steroid hormone synthesis and function. Biochem. Soc. Trans. 2010, 38:54-59.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 54-59
    • Talamillo, A.1    Martin, D.2    Hjerpe, R.3    Sanchez, J.4    Barrio, R.5
  • 49
    • 73249115366 scopus 로고    scopus 로고
    • Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases
    • Beck I.M., Vanden Berghe W., Vermeulen L., Yamamoto K.R., Haegeman G., De Bosscher K. Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases. Endocr. Rev. 2009, 30:830-882.
    • (2009) Endocr. Rev. , vol.30 , pp. 830-882
    • Beck, I.M.1    Vanden Berghe, W.2    Vermeulen, L.3    Yamamoto, K.R.4    Haegeman, G.5    De Bosscher, K.6
  • 50
    • 33750475959 scopus 로고    scopus 로고
    • Cross-talk between nuclear receptors and nuclear factor kappaB
    • De Bosscher K., Vanden Berghe W., Haegeman G. Cross-talk between nuclear receptors and nuclear factor kappaB. Oncogene 2006, 25:6868-6886.
    • (2006) Oncogene , vol.25 , pp. 6868-6886
    • De Bosscher, K.1    Vanden Berghe, W.2    Haegeman, G.3
  • 54
    • 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. USA 2000, 97:14145-14150.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 56
    • 59249093556 scopus 로고    scopus 로고
    • Regulation of transcription factor activity by SUMO modification
    • Ouyang J., Valin A., Gill G. Regulation of transcription factor activity by SUMO modification. Meth. Mol. Biol. 2009, 497:141-152.
    • (2009) Meth. Mol. Biol. , vol.497 , pp. 141-152
    • Ouyang, J.1    Valin, A.2    Gill, G.3
  • 57
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • Gill G. Something about SUMO inhibits transcription. Curr. Opin. Genet. Dev. 2005, 15:536-541.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 536-541
    • Gill, G.1
  • 59
    • 20344384269 scopus 로고    scopus 로고
    • SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin
    • Chalkiadaki A., Talianidis I. SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin. Mol. Cell. Biol. 2005, 25:5095-5105.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5095-5105
    • Chalkiadaki, A.1    Talianidis, I.2
  • 60
    • 13544259457 scopus 로고    scopus 로고
    • The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification
    • Lee M.B., Lebedeva L.A., Suzawa M., Wadekar S.A., Desclozeaux M., Ingraham H.A. The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification. Mol. Cell. Biol. 2005, 25:1879-1890.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1879-1890
    • Lee, M.B.1    Lebedeva, L.A.2    Suzawa, M.3    Wadekar, S.A.4    Desclozeaux, M.5    Ingraham, H.A.6
  • 61
    • 4644354099 scopus 로고    scopus 로고
    • SUMO modification of repression domains modulates function of nuclear receptor 5A1 (steroidogenic factor-1)
    • Chen W.Y., Lee W.C., Hsu N.C., Huang F., Chung B.C. SUMO modification of repression domains modulates function of nuclear receptor 5A1 (steroidogenic factor-1). J. Biol. Chem. 2004, 279:38730-38735.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38730-38735
    • Chen, W.Y.1    Lee, W.C.2    Hsu, N.C.3    Huang, F.4    Chung, B.C.5
  • 62
    • 33846114807 scopus 로고    scopus 로고
    • SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells
    • Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N. SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells. Nat. Struct. Mol. Biol. 2007, 14:68-75.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 68-75
    • Park, S.W.1    Hu, X.2    Gupta, P.3    Lin, Y.P.4    Ha, S.G.5    Wei, L.N.6
  • 64
    • 27644467440 scopus 로고    scopus 로고
    • Sumoylation of the estrogen receptor alpha hinge region regulates its transcriptional activity
    • Sentis S., Le Romancer M., Bianchin C., Rostan M.C., Corbo L. Sumoylation of the estrogen receptor alpha hinge region regulates its transcriptional activity. Mol. Endocrinol. 2005, 19:2671-2684.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 2671-2684
    • Sentis, S.1    Le Romancer, M.2    Bianchin, C.3    Rostan, M.C.4    Corbo, L.5
  • 65
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR
    • Li X., Zhang S., Blander G., Tse J.G., Krieger M., Guarente L. SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell 2007, 28:91-106.
    • (2007) Mol. Cell , vol.28 , pp. 91-106
    • Li, X.1    Zhang, S.2    Blander, G.3    Tse, J.G.4    Krieger, M.5    Guarente, L.6
  • 67
    • 34548363925 scopus 로고    scopus 로고
    • Phosphorylation-dependent sumoylation of estrogen-related receptor alpha1
    • Vu E.H., Kraus R.J., Mertz J.E. Phosphorylation-dependent sumoylation of estrogen-related receptor alpha1. Biochemistry 2007, 46:9795-9804.
    • (2007) Biochemistry , vol.46 , pp. 9795-9804
    • Vu, E.H.1    Kraus, R.J.2    Mertz, J.E.3
  • 68
    • 70349659645 scopus 로고    scopus 로고
    • Sumoylated PPARalpha mediates sex-specific gene repression and protects the liver from estrogen-induced toxicity in mice
    • Leuenberger N., Pradervand S., Wahli W. Sumoylated PPARalpha mediates sex-specific gene repression and protects the liver from estrogen-induced toxicity in mice. J. Clin. Invest. 2009, 119:3138-3148.
    • (2009) J. Clin. Invest. , vol.119 , pp. 3138-3148
    • Leuenberger, N.1    Pradervand, S.2    Wahli, W.3
  • 71
    • 79958248200 scopus 로고    scopus 로고
    • SF-1 in the ventral medial hypothalamic nucleus: a key regulator of homeostasis
    • Nov 24. [Electronic publication ahead of print]
    • Kim K.W., Sohn J.W., Kohno D., Xu Y., Williams K., Elmquist J.K. SF-1 in the ventral medial hypothalamic nucleus: a key regulator of homeostasis. Mol. Cell. Endocrinol. 2010, Nov 24. [Electronic publication ahead of print].
    • (2010) Mol. Cell. Endocrinol.
    • Kim, K.W.1    Sohn, J.W.2    Kohno, D.3    Xu, Y.4    Williams, K.5    Elmquist, J.K.6
  • 73
    • 73449092854 scopus 로고    scopus 로고
    • SUMO engages multiple corepressors to regulate chromatin structure and transcription
    • Ouyang J., Gill G. SUMO engages multiple corepressors to regulate chromatin structure and transcription. Epigenetics 2009, 4:440-444.
    • (2009) Epigenetics , vol.4 , pp. 440-444
    • Ouyang, J.1    Gill, G.2
  • 74
    • 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. Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol. Cell 2009, 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
  • 75
    • 40849150778 scopus 로고    scopus 로고
    • Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen
    • Stielow B., Sapetschnig A., Kruger I., Kunert N., Brehm A., Boutros M., Suske G. Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen. Mol. Cell 2008, 29:742-754.
    • (2008) Mol. Cell , vol.29 , pp. 742-754
    • Stielow, B.1    Sapetschnig, A.2    Kruger, I.3    Kunert, N.4    Brehm, A.5    Boutros, M.6    Suske, G.7
  • 76
    • 70350223560 scopus 로고    scopus 로고
    • Transcriptional suppression by transient recruitment of ARIP4 to sumoylated nuclear receptor Ad4BP/SF-1
    • Ogawa H., Komatsu T., Hiraoka Y., Morohashi K. Transcriptional suppression by transient recruitment of ARIP4 to sumoylated nuclear receptor Ad4BP/SF-1. Mol. Biol. Cell 2009, 20:4235-4245.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4235-4245
    • Ogawa, H.1    Komatsu, T.2    Hiraoka, Y.3    Morohashi, K.4
  • 77
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O. SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep. 2007, 8:550-555.
    • (2007) EMBO Rep. , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 79
    • 63049083734 scopus 로고    scopus 로고
    • A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death
    • Saijo K., Winner B., Carson C.T., Collier J.G., Boyer L., Rosenfeld M.G., Gage F.H., Glass C.K. A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death. Cell 2009, 137:47-59.
    • (2009) Cell , vol.137 , pp. 47-59
    • Saijo, K.1    Winner, B.2    Carson, C.T.3    Collier, J.G.4    Boyer, L.5    Rosenfeld, M.G.6    Gage, F.H.7    Glass, C.K.8
  • 80
    • 77951918926 scopus 로고    scopus 로고
    • Macrophages, inflammation, and insulin resistance
    • Olefsky J.M., Glass C.K. Macrophages, inflammation, and insulin resistance. Annu. Rev. Physiol. 2010, 72:219-246.
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 219-246
    • Olefsky, J.M.1    Glass, C.K.2
  • 81
    • 61449229273 scopus 로고    scopus 로고
    • Minireview: latest perspectives on antiinflammatory actions of glucocorticoids
    • De Bosscher K., Haegeman G. Minireview: latest perspectives on antiinflammatory actions of glucocorticoids. Mol. Endocrinol. 2009, 23:281-291.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 281-291
    • De Bosscher, K.1    Haegeman, G.2
  • 82
    • 33748702268 scopus 로고    scopus 로고
    • Nuclear receptors versus inflammation: mechanisms of transrepression
    • Pascual G., Glass C.K. Nuclear receptors versus inflammation: mechanisms of transrepression. Trends Endocrinol. Metab. TEM 2006, 17:321-327.
    • (2006) Trends Endocrinol. Metab. TEM , vol.17 , pp. 321-327
    • Pascual, G.1    Glass, C.K.2
  • 84
    • 8444233254 scopus 로고    scopus 로고
    • Nuclear receptors in macrophage biology: at the crossroads of lipid metabolism and inflammation
    • Castrillo A., Tontonoz P. Nuclear receptors in macrophage biology: at the crossroads of lipid metabolism and inflammation. Annu. Rev. Cell Dev. Biol. 2004, 20:455-480.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 455-480
    • Castrillo, A.1    Tontonoz, P.2
  • 85
    • 33644651160 scopus 로고    scopus 로고
    • Liver X receptors as integrators of metabolic and inflammatory signaling
    • Zelcer N., Tontonoz P. Liver X receptors as integrators of metabolic and inflammatory signaling. J. Clin. Invest. 2006, 116:607-614.
    • (2006) J. Clin. Invest. , vol.116 , pp. 607-614
    • Zelcer, N.1    Tontonoz, P.2
  • 86
    • 47949094965 scopus 로고    scopus 로고
    • Integration of metabolism and inflammation by lipid-activated nuclear receptors
    • Bensinger S.J., Tontonoz P. Integration of metabolism and inflammation by lipid-activated nuclear receptors. Nature 2008, 454:470-477.
    • (2008) Nature , vol.454 , pp. 470-477
    • Bensinger, S.J.1    Tontonoz, P.2
  • 88
    • 33748669670 scopus 로고    scopus 로고
    • Liver receptor homolog 1 is a negative regulator of the hepatic acute-phase response
    • Venteclef N., Smith J.C., Goodwin B., Delerive P. Liver receptor homolog 1 is a negative regulator of the hepatic acute-phase response. Mol. Cell. Biol. 2006, 26:6799-6807.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 6799-6807
    • Venteclef, N.1    Smith, J.C.2    Goodwin, B.3    Delerive, P.4
  • 89
    • 33845635077 scopus 로고    scopus 로고
    • A nuclear receptor corepressor-dependent pathway mediates suppression of cytokine-induced C-reactive protein gene expression by liver X receptor
    • Blaschke F., Takata Y., Caglayan E., Collins A., Tontonoz P., Hsueh W.A., Tangirala R.K. A nuclear receptor corepressor-dependent pathway mediates suppression of cytokine-induced C-reactive protein gene expression by liver X receptor. Circ. Res. 2006, 99:e88-e99.
    • (2006) Circ. Res. , vol.99
    • Blaschke, F.1    Takata, Y.2    Caglayan, E.3    Collins, A.4    Tontonoz, P.5    Hsueh, W.A.6    Tangirala, R.K.7
  • 90
    • 0036211850 scopus 로고    scopus 로고
    • The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2
    • Zhang J., Kalkum M., Chait B.T., Roeder R.G. The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol. Cell 2002, 9:611-623.
    • (2002) Mol. Cell , vol.9 , pp. 611-623
    • Zhang, J.1    Kalkum, M.2    Chait, B.T.3    Roeder, R.G.4
  • 93
    • 70349191359 scopus 로고    scopus 로고
    • Differential SUMOylation of LXRalpha and LXRbeta mediates transrepression of STAT1 inflammatory signaling in IFN-gamma-stimulated brain astrocytes
    • Lee J.H., Park S.M., Kim O.S., Lee C.S., Woo J.H., Park S.J., Joe E.H., Jou I. Differential SUMOylation of LXRalpha and LXRbeta mediates transrepression of STAT1 inflammatory signaling in IFN-gamma-stimulated brain astrocytes. Mol. Cell 2009, 35:806-817.
    • (2009) Mol. Cell , vol.35 , pp. 806-817
    • Lee, J.H.1    Park, S.M.2    Kim, O.S.3    Lee, C.S.4    Woo, J.H.5    Park, S.J.6    Joe, E.H.7    Jou, I.8
  • 94
    • 63049122784 scopus 로고    scopus 로고
    • Cooperative NCoR/SMRT interactions establish a corepressor-based strategy for integration of inflammatory and anti-inflammatory signaling pathways
    • Ghisletti S., Huang W., Jepsen K., Benner C., Hardiman G., Rosenfeld M.G., Glass C.K. Cooperative NCoR/SMRT interactions establish a corepressor-based strategy for integration of inflammatory and anti-inflammatory signaling pathways. Genes Dev. 2009, 23:681-693.
    • (2009) Genes Dev. , vol.23 , pp. 681-693
    • Ghisletti, S.1    Huang, W.2    Jepsen, K.3    Benner, C.4    Hardiman, G.5    Rosenfeld, M.G.6    Glass, C.K.7
  • 96
    • 36049034344 scopus 로고    scopus 로고
    • Anti-inflammatory actions of PPAR ligands: new insights on cellular and molecular mechanisms
    • Straus D.S., Glass C.K. Anti-inflammatory actions of PPAR ligands: new insights on cellular and molecular mechanisms. Trends Immunol. 2007, 28:551-558.
    • (2007) Trends Immunol. , vol.28 , pp. 551-558
    • Straus, D.S.1    Glass, C.K.2
  • 99
    • 33751009392 scopus 로고    scopus 로고
    • Identification of small molecule agonists of the orphan nuclear receptors liver receptor homolog-1 and steroidogenic factor-1
    • Whitby R.J., Dixon S., Maloney P.R., Delerive P., Goodwin B.J., Parks D.J., Willson T.M. Identification of small molecule agonists of the orphan nuclear receptors liver receptor homolog-1 and steroidogenic factor-1. J. Med. Chem. 2006, 49:6652-6655.
    • (2006) J. Med. Chem. , vol.49 , pp. 6652-6655
    • Whitby, R.J.1    Dixon, S.2    Maloney, P.R.3    Delerive, P.4    Goodwin, B.J.5    Parks, D.J.6    Willson, T.M.7
  • 102
    • 24144459909 scopus 로고    scopus 로고
    • Thematic review series: The immune system and atherogenesis. Lipoprotein-associated inflammatory proteins: markers or mediators of cardiovascular disease?
    • Chait A., Han C.Y., Oram J.F., Heinecke J.W. Thematic review series: The immune system and atherogenesis. Lipoprotein-associated inflammatory proteins: markers or mediators of cardiovascular disease?. J. Lipid Res. 2005, 46:389-403.
    • (2005) J. Lipid Res. , vol.46 , pp. 389-403
    • Chait, A.1    Han, C.Y.2    Oram, J.F.3    Heinecke, J.W.4
  • 103
    • 27844545767 scopus 로고    scopus 로고
    • Signalling role of adipose tissue: adipokines and inflammation in obesity
    • Trayhurn P., Wood I.S. Signalling role of adipose tissue: adipokines and inflammation in obesity. Biochem. Soc. Trans. 2005, 33:1078-1081.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1078-1081
    • Trayhurn, P.1    Wood, I.S.2
  • 105
    • 29144461456 scopus 로고    scopus 로고
    • Thiazolidinediones: pleiotropic drugs with potent anti-inflammatory properties for tissue protection
    • Buckingham R.E. Thiazolidinediones: pleiotropic drugs with potent anti-inflammatory properties for tissue protection. Hepatol. Res. 2005, 33:167-170.
    • (2005) Hepatol. Res. , vol.33 , pp. 167-170
    • Buckingham, R.E.1
  • 106
    • 77149159568 scopus 로고    scopus 로고
    • The bile acid receptor FXR is a modulator of intestinal innate immunity
    • Vavassori P., Mencarelli A., Renga B., Distrutti E., Fiorucci S. The bile acid receptor FXR is a modulator of intestinal innate immunity. J. Immunol. 2009, 183:6251-6261.
    • (2009) J. Immunol. , vol.183 , pp. 6251-6261
    • Vavassori, P.1    Mencarelli, A.2    Renga, B.3    Distrutti, E.4    Fiorucci, S.5
  • 107
    • 34447327216 scopus 로고    scopus 로고
    • Gender disparity in liver cancer due to sex differences in MyD88-dependent IL-6 production
    • Naugler W.E., Sakurai T., Kim S., Maeda S., Kim K., Elsharkawy A.M., Karin M. Gender disparity in liver cancer due to sex differences in MyD88-dependent IL-6 production. Science 2007, 317:121-124.
    • (2007) Science , vol.317 , pp. 121-124
    • Naugler, W.E.1    Sakurai, T.2    Kim, S.3    Maeda, S.4    Kim, K.5    Elsharkawy, A.M.6    Karin, M.7
  • 108
    • 77952955740 scopus 로고    scopus 로고
    • Sex steroids as inflammatory regulators
    • Gilliver S.C. Sex steroids as inflammatory regulators. J. Steroid Biochem. Mol. Biol. 2010, 120:105-115.
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.120 , pp. 105-115
    • Gilliver, S.C.1
  • 110
    • 67349245212 scopus 로고    scopus 로고
    • Impact of sex steroids on neuroinflammatory processes and experimental multiple sclerosis
    • Kipp M., Beyer C. Impact of sex steroids on neuroinflammatory processes and experimental multiple sclerosis. Front. Neuroendocrinol. 2009, 30:188-200.
    • (2009) Front. Neuroendocrinol. , vol.30 , pp. 188-200
    • Kipp, M.1    Beyer, C.2
  • 111
    • 58149149885 scopus 로고    scopus 로고
    • Liver receptor homolog-1 localization in the nuclear body is regulated by sumoylation and cAMP signaling in rat granulosa cells
    • Yang F.M., Pan C.T., Tsai H.M., Chiu T.W., Wu M.L., Hu M.C. Liver receptor homolog-1 localization in the nuclear body is regulated by sumoylation and cAMP signaling in rat granulosa cells. FEBS J. 2009, 276:425-436.
    • (2009) FEBS J. , vol.276 , pp. 425-436
    • Yang, F.M.1    Pan, C.T.2    Tsai, H.M.3    Chiu, T.W.4    Wu, M.L.5    Hu, M.C.6
  • 112
    • 5044236130 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergy control motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9
    • Komatsu T., Mizusaki H., Mukai T., Ogawa H., Baba D., Shirakawa M., Hatakeyama S., Nakayama K.I., Yamamoto H., Kikuchi A., Morohashi K. Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergy control motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9. Mol. Endocrinol. 2004, 18:2451-2462.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2451-2462
    • Komatsu, T.1    Mizusaki, H.2    Mukai, T.3    Ogawa, H.4    Baba, D.5    Shirakawa, M.6    Hatakeyama, S.7    Nakayama, K.I.8    Yamamoto, H.9    Kikuchi, A.10    Morohashi, K.11
  • 113
    • 57849135455 scopus 로고    scopus 로고
    • Retinoid X receptor and peroxisome proliferator-activated receptor-gamma agonists cooperate to inhibit matrix metalloproteinase gene expression
    • Burrage P.S., Schmucker A.C., Ren Y., Sporn M.B., Brinckerhoff C.E. Retinoid X receptor and peroxisome proliferator-activated receptor-gamma agonists cooperate to inhibit matrix metalloproteinase gene expression. Arthritis Res. Ther. 2008, 10:R139.
    • (2008) Arthritis Res. Ther. , vol.10
    • Burrage, P.S.1    Schmucker, A.C.2    Ren, Y.3    Sporn, M.B.4    Brinckerhoff, C.E.5
  • 114
    • 33750089739 scopus 로고    scopus 로고
    • Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1
    • Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H., Baek S.H., Bang O.S., Chung C.H. Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1. J. Biol. Chem. 2006, 281:30669-30677.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30669-30677
    • Choi, S.J.1    Chung, S.S.2    Rho, E.J.3    Lee, H.W.4    Lee, M.H.5    Choi, H.S.6    Seol, J.H.7    Baek, S.H.8    Bang, O.S.9    Chung, C.H.10
  • 115
    • 77949878458 scopus 로고    scopus 로고
    • SUMOylation of human peroxisome proliferator-activated receptor alpha inhibits its trans-activity through the recruitment of the nuclear corepressor NCoR
    • Pourcet B., Pineda-Torra I., Derudas B., Staels B., Glineur C. SUMOylation of human peroxisome proliferator-activated receptor alpha inhibits its trans-activity through the recruitment of the nuclear corepressor NCoR. J. Biol. Chem. 2010, 285:5983-5992.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5983-5992
    • Pourcet, B.1    Pineda-Torra, I.2    Derudas, B.3    Staels, B.4    Glineur, C.5
  • 116
    • 3142716146 scopus 로고    scopus 로고
    • Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification
    • Ohshima T., Koga H., Shimotohno K. Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification. J. Biol. Chem. 2004, 279:29551-29557.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29551-29557
    • Ohshima, T.1    Koga, H.2    Shimotohno, K.3
  • 117
    • 54049147721 scopus 로고    scopus 로고
    • Sumoylation of peroxisome proliferator-activated receptor gamma by apoptotic cells prevents lipopolysaccharide-induced NCoR removal from kappaB binding sites mediating transrepression of proinflammatory cytokines
    • Jennewein C., Kuhn A.M., Schmidt M.V., Meilladec-Jullig V., von Knethen A., Gonzalez F.J., Brune B. Sumoylation of peroxisome proliferator-activated receptor gamma by apoptotic cells prevents lipopolysaccharide-induced NCoR removal from kappaB binding sites mediating transrepression of proinflammatory cytokines. J. Immunol. 2008, 181:5646-5652.
    • (2008) J. Immunol. , vol.181 , pp. 5646-5652
    • Jennewein, C.1    Kuhn, A.M.2    Schmidt, M.V.3    Meilladec-Jullig, V.4    von Knethen, A.5    Gonzalez, F.J.6    Brune, B.7
  • 119
    • 78149263436 scopus 로고    scopus 로고
    • Pregnane X receptor is SUMOylated to repress the inflammatory response
    • Hu G., Xu C., Staudinger J.L. Pregnane X receptor is SUMOylated to repress the inflammatory response. J. Pharmacol. Exp. Ther. 2010, 335:342-350.
    • (2010) J. Pharmacol. Exp. Ther. , vol.335 , pp. 342-350
    • Hu, G.1    Xu, C.2    Staudinger, J.L.3
  • 120
    • 0036291475 scopus 로고    scopus 로고
    • PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases
    • Kotaja N., Karvonen U., Janne O.A., Palvimo J.J. PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases. Mol. Cell. Biol. 2002, 22:5222-5234.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5222-5234
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 121
    • 2542487192 scopus 로고    scopus 로고
    • Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements
    • Callewaert L., Verrijdt G., Haelens A., Claessens F. Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements. Mol. Endocrinol. 2004, 18:1438-1449.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1438-1449
    • Callewaert, L.1    Verrijdt, G.2    Haelens, A.3    Claessens, F.4
  • 122
    • 69249090927 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation
    • Mukherjee S., Thomas M., Dadgar N., Lieberman A.P., Iniguez-Lluhi J.A. Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation. J. Biol. Chem. 2009, 284:21296-21306.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21296-21306
    • Mukherjee, S.1    Thomas, M.2    Dadgar, N.3    Lieberman, A.P.4    Iniguez-Lluhi, J.A.5
  • 123
    • 0347994898 scopus 로고    scopus 로고
    • Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy
    • Holmstrom S., Van Antwerp M.E., Iniguez-Lluhi J.A. Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy. Proc. Natl Acad. Sci. USA 2003, 100:15758-15763.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15758-15763
    • Holmstrom, S.1    Van Antwerp, M.E.2    Iniguez-Lluhi, J.A.3
  • 124
    • 50649103009 scopus 로고    scopus 로고
    • SUMO-mediated inhibition of glucocorticoid receptor synergistic activity depends on stable assembly at the promoter but not on DAXX
    • Holmstrom S.R., Chupreta S., So A.Y., Iniguez-Lluhi J.A. SUMO-mediated inhibition of glucocorticoid receptor synergistic activity depends on stable assembly at the promoter but not on DAXX. Mol. Endocrinol. 2008, 22:2061-2075.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 2061-2075
    • Holmstrom, S.R.1    Chupreta, S.2    So, A.Y.3    Iniguez-Lluhi, J.A.4
  • 125
    • 36849096094 scopus 로고    scopus 로고
    • Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells
    • Daniel A.R., Faivre E.J., Lange C.A. Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells. Mol. Endocrinol. 2007, 21:2890-2906.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2890-2906
    • Daniel, A.R.1    Faivre, E.J.2    Lange, C.A.3
  • 126
    • 0037119457 scopus 로고    scopus 로고
    • The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1
    • Kotaja N., Karvonen U., Janne O.A., Palvimo J.J. The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1. J. Biol. Chem. 2002, 277:30283-30288.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30283-30288
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 127
    • 70350031566 scopus 로고    scopus 로고
    • SUMOylation attenuates the function of PGC-1alpha
    • Rytinki M.M., Palvimo J.J. SUMOylation attenuates the function of PGC-1alpha. J. Biol. Chem. 2009, 284:26184-26193.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26184-26193
    • Rytinki, M.M.1    Palvimo, J.J.2
  • 128
    • 45549093122 scopus 로고    scopus 로고
    • SUMOylation modulates the transcription repressor function of RIP140
    • Rytinki M.M., Palvimo J.J. SUMOylation modulates the transcription repressor function of RIP140. J. Biol. Chem. 2008, 283:11586-11595.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11586-11595
    • Rytinki, M.M.1    Palvimo, J.J.2
  • 130
    • 33745393452 scopus 로고    scopus 로고
    • SUMOylation of the corepressor N-CoR modulates its capacity to repress transcription
    • Tiefenbach J., Novac N., Ducasse M., Eck M., Melchior F., Heinzel T. SUMOylation of the corepressor N-CoR modulates its capacity to repress transcription. Mol. Biol. Cell 2006, 17:1643-1651.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1643-1651
    • Tiefenbach, J.1    Novac, N.2    Ducasse, M.3    Eck, M.4    Melchior, F.5    Heinzel, T.6
  • 131
    • 2942735131 scopus 로고    scopus 로고
    • SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1
    • Cheng J., Wang D., Wang Z., Yeh E.T. SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol. Cell. Biol. 2004, 24:6021-6028.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6021-6028
    • Cheng, J.1    Wang, D.2    Wang, Z.3    Yeh, E.T.4
  • 133
    • 31544475671 scopus 로고    scopus 로고
    • Biochemical characterization of androgen receptor-interacting protein 4
    • Domanskyi A., Virtanen K.T., Palvimo J.J., Janne O.A. Biochemical characterization of androgen receptor-interacting protein 4. Biochem. J. 2006, 393:789-795.
    • (2006) Biochem. J. , vol.393 , pp. 789-795
    • Domanskyi, A.1    Virtanen, K.T.2    Palvimo, J.J.3    Janne, O.A.4
  • 134
    • 44949181877 scopus 로고    scopus 로고
    • SUMOylation of Kruppel-like transcription factor 5 acts as a molecular switch in transcriptional programs of lipid metabolism involving PPAR-delta
    • Oishi Y., Manabe I., Tobe K., Ohsugi M., Kubota T., Fujiu K., Maemura K., Kubota N., Kadowaki T., Nagai R. SUMOylation of Kruppel-like transcription factor 5 acts as a molecular switch in transcriptional programs of lipid metabolism involving PPAR-delta. Nat. Med. 2008, 14:656-666.
    • (2008) Nat. Med. , vol.14 , pp. 656-666
    • Oishi, Y.1    Manabe, I.2    Tobe, K.3    Ohsugi, M.4    Kubota, T.5    Fujiu, K.6    Maemura, K.7    Kubota, N.8    Kadowaki, T.9    Nagai, R.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.