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Volumn 8, Issue 1, 2013, Pages

PIASγ Enhanced SUMO-2 Modification of Nurr1 Activation-Function-1 Domain Limits Nurr1 Transcriptional Synergy

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; LYSINE; NUCLEAR RECEPTOR RELATED FACTOR 1; PIAS GAMMA PROTEIN; SUMO 2 PROTEIN; SUMO LIGASE; SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84872843475     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055035     Document Type: Article
Times cited : (24)

References (35)
  • 1
    • 5544325468 scopus 로고    scopus 로고
    • Nurr1, an orphan nuclear receptor with essential functions in developing dopamine cells
    • Perlmann T, Wallén-Mackenzie A, (2004) Nurr1, an orphan nuclear receptor with essential functions in developing dopamine cells. Cell Tissue Res 318: 45-52.
    • (2004) Cell Tissue Res , vol.318 , pp. 45-52
    • Perlmann, T.1    Wallén-Mackenzie, A.2
  • 2
    • 33747196651 scopus 로고    scopus 로고
    • The NR4A subgroup: immediate early response genes with pleiotropic physiological roles
    • Maxwell MA, Muscat GE, (2006) The NR4A subgroup: immediate early response genes with pleiotropic physiological roles. Nucl Recept Signal 4: e002.
    • (2006) Nucl Recept Signal , vol.4
    • Maxwell, M.A.1    Muscat, G.E.2
  • 3
  • 4
    • 0038526314 scopus 로고    scopus 로고
    • Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors
    • Wang Z, Benoit G, Liu J, Prasad S, Aarnisalo P, et al. (2003) Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors. Nature 423: 555-560.
    • (2003) Nature , vol.423 , pp. 555-560
    • Wang, Z.1    Benoit, G.2    Liu, J.3    Prasad, S.4    Aarnisalo, P.5
  • 5
    • 0033601290 scopus 로고    scopus 로고
    • Activity of the Nurr1 carboxy-terminal domain depends on cell type and integrity of the activation function 2
    • Castro DS, Arvidsson M, Bondesson-Bolin M, Perlmann T, (1999) Activity of the Nurr1 carboxy-terminal domain depends on cell type and integrity of the activation function 2. J Biol Chem 274: 37483-37490.
    • (1999) J Biol Chem , vol.274 , pp. 37483-37490
    • Castro, D.S.1    Arvidsson, M.2    Bondesson-Bolin, M.3    Perlmann, T.4
  • 6
    • 37749037140 scopus 로고    scopus 로고
    • PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription
    • Palvimo JJ, (2007) PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription. Biochem Soc Trans 35: 1405-1048.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1048-1405
    • Palvimo, J.J.1
  • 7
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: new partners in transcriptional regulation
    • Schmidt D, Müller S, (2003) PIAS/SUMO: new partners in transcriptional regulation. Cell Mol Life Sci 60: 2561-2574.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2561-2574
    • Schmidt, D.1    Müller, S.2
  • 8
    • 0345826086 scopus 로고    scopus 로고
    • PIASgamma represses the transcriptional activation induced by the nuclear receptor Nurr1
    • Galleguillos D, Vecchiola A, Fuentealba JA, Ojeda V, Alvarez K, et al. (2004) PIASgamma represses the transcriptional activation induced by the nuclear receptor Nurr1. J Biol Chem 279: 2005-2011.
    • (2004) J Biol Chem , vol.279 , pp. 2005-2011
    • Galleguillos, D.1    Vecchiola, A.2    Fuentealba, J.A.3    Ojeda, V.4    Alvarez, K.5
  • 10
    • 63549129144 scopus 로고    scopus 로고
    • SUMOylation and De-SUMOylation: wrestling with life's processes
    • Yeh ET, (2009) SUMOylation and De-SUMOylation: wrestling with life's processes. J Biol Chem 284: 8223-8227.
    • (2009) J Biol Chem , vol.284 , pp. 8223-8227
    • Yeh, E.T.1
  • 11
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson ES, (2004) Protein modification by SUMO. Annu Rev Biochem 73: 355-382.
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 12
    • 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
  • 13
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H, Karvonen U, Janne OA, Palvimo JJ, (2000) Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc Natl Acad Sci USA 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
  • 14
    • 0033859780 scopus 로고    scopus 로고
    • A common motif within the negative regulatory regions of multiple factors inhibits their transcripcional synergy
    • Iñiguez-Lluhí JA, Pearce D, (2000) A common motif within the negative regulatory regions of multiple factors inhibits their transcripcional synergy. Mol Cell Biol 20: 6040-6050.
    • (2000) Mol Cell Biol , vol.20 , pp. 6040-6050
    • Iñiguez-Lluhí, J.A.1    Pearce, D.2
  • 15
    • 0028842908 scopus 로고
    • Regulation of the Nur77 orphan steroid receptor in activation-induced apoptosis
    • Woronicz JD, Lina A, Calnan BJ, Szychowski S, Cheng L, et al. (1995) Regulation of the Nur77 orphan steroid receptor in activation-induced apoptosis. Mol Cell Biol 15: 6364-6376.
    • (1995) Mol Cell Biol , vol.15 , pp. 6364-6376
    • Woronicz, J.D.1    Lina, A.2    Calnan, B.J.3    Szychowski, S.4    Cheng, L.5
  • 16
    • 0346422441 scopus 로고    scopus 로고
    • Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1
    • Bailey D, O'Hare P, (2004) Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1. J Biol Chem 279: 692-703.
    • (2004) J Biol Chem , vol.279 , pp. 692-703
    • Bailey, D.1    O'Hare, P.2
  • 18
    • 79960846307 scopus 로고    scopus 로고
    • Corticotropin-releasing factor binding protein enters the regulated secretor pathway in neuroendocrine cells and cortical neurons
    • Blanco EH, Zúñiga JP, Andrés ME, Alvarez AR, Gysling K, (2011) Corticotropin-releasing factor binding protein enters the regulated secretor pathway in neuroendocrine cells and cortical neurons. Neuropeptides 45: 273-279.
    • (2011) Neuropeptides , vol.45 , pp. 273-279
    • Blanco, E.H.1    Zúñiga, J.P.2    Andrés, M.E.3    Alvarez, A.R.4    Gysling, K.5
  • 19
    • 0029935163 scopus 로고    scopus 로고
    • Partial colocalization of glucocorticoid and mineralocorticoid receptors in discrete compartments in nuclei of rat hippocampus neurons
    • van Steensel B, van Binnendijk EP, Hornsby CD, van der Voort HT, Krozowski ZS, et al. (1996) Partial colocalization of glucocorticoid and mineralocorticoid receptors in discrete compartments in nuclei of rat hippocampus neurons. J Cell Sci. 109: 787-792.
    • (1996) J Cell Sci , vol.109 , pp. 787-792
    • van Steensel, B.1    van Binnendijk, E.P.2    Hornsby, C.D.3    van der Voort, H.T.4    Krozowski, Z.S.5
  • 20
    • 33744523786 scopus 로고    scopus 로고
    • PIASγ-mediated repression of the Ets-1 is independent of its sumoylation
    • Nishida T, Terashima M, Fukami K, (2006) PIASγ-mediated repression of the Ets-1 is independent of its sumoylation. Biochem Biophys Res Commun 345: 1536-1546.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 1536-1546
    • Nishida, T.1    Terashima, M.2    Fukami, K.3
  • 21
    • 1942502336 scopus 로고    scopus 로고
    • The coactivator LXXLL nuclear receptor recognition motif
    • Savkur RS, Burris TP, (2004) The coactivator LXXLL nuclear receptor recognition motif. J Pept Res. 63: 207-212.
    • (2004) J Pept Res , vol.63 , pp. 207-212
    • Savkur, R.S.1    Burris, T.P.2
  • 22
    • 70349857799 scopus 로고    scopus 로고
    • Generation of dopamine neurons with improved cell survival and phenotype maintenance using a degradation-resistant nurr1 mutant
    • Jo AY, Kim MY, Lee HS, Rhee YH, Lee JE, et al. (2009) Generation of dopamine neurons with improved cell survival and phenotype maintenance using a degradation-resistant nurr1 mutant. Stem Cells 27: 2238-2246.
    • (2009) Stem Cells , vol.27 , pp. 2238-2246
    • Jo, A.Y.1    Kim, M.Y.2    Lee, H.S.3    Rhee, Y.H.4    Lee, J.E.5
  • 23
    • 84866053988 scopus 로고    scopus 로고
    • The in vivo role of Androgen Receptor SUMOylation as revealed by androgen insensitivity syndrome and prostate cancer mutations targeting the proline/glycine residues of synergy control motifs
    • Mukherjee S, Cruz-Rodríguez O, Bolton E, Iñiguez-Lluhí JA, (2012) The in vivo role of Androgen Receptor SUMOylation as revealed by androgen insensitivity syndrome and prostate cancer mutations targeting the proline/glycine residues of synergy control motifs. J Biol Chem 287: 31195-31206.
    • (2012) J Biol Chem , vol.287 , pp. 31195-31206
    • Mukherjee, S.1    Cruz-Rodríguez, O.2    Bolton, E.3    Iñiguez-Lluhí, J.A.4
  • 24
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau JR, Lima CD, (2010) The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat Rev Mol Cell Biol 11: 861-871.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 25
    • 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 CT, Collier JG, Boyer L, et al. (2009) A Nurr1/CoREST pathway in microglia and astrocytes protects dopaminergic neurons from inflammation-induced death. Cell 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
  • 26
    • 66149124844 scopus 로고    scopus 로고
    • Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation
    • Abdel-Hafiz H, Dudevoir ML, Horwitz KB, (2009) Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation. J Biol Chem 284: 9099-9108.
    • (2009) J Biol Chem , vol.284 , pp. 9099-9108
    • Abdel-Hafiz, H.1    Dudevoir, M.L.2    Horwitz, K.B.3
  • 27
    • 84859941402 scopus 로고    scopus 로고
    • PIAS1 is a GATA4 SUMO ligase that regulates GATA4-dependent intestinal promoters independent of SUMO ligase activity and GATA4 sumoylation
    • Belaguli NS, Zhang M, García AH, Berger DH, (2012) PIAS1 is a GATA4 SUMO ligase that regulates GATA4-dependent intestinal promoters independent of SUMO ligase activity and GATA4 sumoylation. PLoS One 7: e35717.
    • (2012) PLoS One , vol.7
    • Belaguli, N.S.1    Zhang, M.2    García, A.H.3    Berger, D.H.4
  • 28
    • 80053945453 scopus 로고    scopus 로고
    • SUMOYlation of the Forkhead transcription factor FOXL2 promotes its stabilization/activation through transient recruitment to PML bodies
    • Georges A, Benayoun BA, Marongiu M, Dipietromaria A, L'Hôte D, et al. (2011) SUMOYlation of the Forkhead transcription factor FOXL2 promotes its stabilization/activation through transient recruitment to PML bodies. PLoS One 6: e25463.
    • (2011) PLoS One , vol.6
    • Georges, A.1    Benayoun, B.A.2    Marongiu, M.3    Dipietromaria, A.4    L'Hôte, D.5
  • 29
    • 0347994898 scopus 로고    scopus 로고
    • Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy
    • Holmstrom S, Van Antwerp ME, Iñiguez-Lluhi JA, (2003) Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy. Proc Natl Acad Sci USA 100: 15758-15763.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15758-15763
    • Holmstrom, S.1    Van Antwerp, M.E.2    Iñiguez-Lluhi, J.A.3
  • 30
    • 84858713890 scopus 로고    scopus 로고
    • Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation
    • Abdel-Hafiz HA, Horwitz KB, (2012) Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation. BMC Mol Biol 13: 10.
    • (2012) BMC Mol Biol , vol.13 , pp. 10
    • Abdel-Hafiz, H.A.1    Horwitz, K.B.2
  • 31
    • 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 SR, Chupreta S, So AY, Iñiguez-Lluhí JA, (2008) SUMO-mediated inhibition of glucocorticoid receptor synergistic activity depends on stable assembly at the promoter but not on DAXX. Mol. Endocrinol 22: 2061-2075.
    • (2008) Mol Endocrinol , vol.22 , pp. 2061-2075
    • Holmstrom, S.R.1    Chupreta, S.2    So, A.Y.3    Iñiguez-Lluhí, J.A.4
  • 32
    • 40849126935 scopus 로고    scopus 로고
    • Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif
    • Tremblay AM, Wilson BJ, Yang XJ, Giguère V, (2008) Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif. Mol Endocrinol 22: 570-584.
    • (2008) Mol Endocrinol , vol.22 , pp. 570-584
    • Tremblay, A.M.1    Wilson, B.J.2    Yang, X.J.3    Giguère, V.4
  • 33
    • 0037660209 scopus 로고    scopus 로고
    • Orphan nuclear receptor Nurr1 directly transactivates the promoter activity of the tyrosine hydroxylase gene in a cell-specific manner
    • Kim KS, Kim CH, Hwang DY, Seo H, Chung S, et al. (2003) Orphan nuclear receptor Nurr1 directly transactivates the promoter activity of the tyrosine hydroxylase gene in a cell-specific manner. J Neurochem 85: 622-634.
    • (2003) J Neurochem , vol.85 , pp. 622-634
    • Kim, K.S.1    Kim, C.H.2    Hwang, D.Y.3    Seo, H.4    Chung, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.