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Volumn 24, Issue 1, 2013, Pages 1-12

SUMO: A Multifaceted Modifier of Chromatin Structure and Function

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE; HISTONE DEACETYLASE; POLYCOMB GROUP PROTEIN; REPETITIVE DNA; SUMO PROTEIN;

EID: 84872413578     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2012.11.020     Document Type: Review
Times cited : (213)

References (136)
  • 1
    • 58149299642 scopus 로고    scopus 로고
    • Covalent conjugation of Groucho with SUMO-1 modulates its corepressor activity
    • Ahn J.W., Lee Y.A., Ahn J.H., Choi C.Y. Covalent conjugation of Groucho with SUMO-1 modulates its corepressor activity. Biochem. Biophys. Res. Commun. 2009, 379:160-165.
    • (2009) Biochem. Biophys. Res. Commun. , vol.379 , pp. 160-165
    • Ahn, J.W.1    Lee, Y.A.2    Ahn, J.H.3    Choi, C.Y.4
  • 3
    • 84857748099 scopus 로고    scopus 로고
    • Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2
    • Armstrong A.A., Mohideen F., Lima C.D. Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2. Nature 2012, 483:59-63.
    • (2012) Nature , vol.483 , pp. 59-63
    • Armstrong, A.A.1    Mohideen, F.2    Lima, C.D.3
  • 4
    • 9444260454 scopus 로고    scopus 로고
    • Distinct in vivo dynamics of vertebrate SUMO paralogues
    • Ayaydin F., Dasso M. Distinct in vivo dynamics of vertebrate SUMO paralogues. Mol. Biol. Cell 2004, 15:5208-5218.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5208-5218
    • Ayaydin, F.1    Dasso, M.2
  • 5
    • 0242509262 scopus 로고    scopus 로고
    • SUMO-2/3 regulates topoisomerase II in mitosis
    • Azuma Y., Arnaoutov A., Dasso M. SUMO-2/3 regulates topoisomerase II in mitosis. J. Cell Biol. 2003, 163:477-487.
    • (2003) J. Cell Biol. , vol.163 , pp. 477-487
    • Azuma, Y.1    Arnaoutov, A.2    Dasso, M.3
  • 6
    • 21844437072 scopus 로고    scopus 로고
    • PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes
    • Azuma Y., Arnaoutov A., Anan T., Dasso M. PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes. EMBO J. 2005, 24:2172-2182.
    • (2005) EMBO J. , vol.24 , pp. 2172-2182
    • Azuma, Y.1    Arnaoutov, A.2    Anan, T.3    Dasso, M.4
  • 8
    • 80054080265 scopus 로고    scopus 로고
    • Polycomb group proteins: repression in 3D
    • Bantignies F., Cavalli G. Polycomb group proteins: repression in 3D. Trends Genet. 2011, 27:454-464.
    • (2011) Trends Genet. , vol.27 , pp. 454-464
    • Bantignies, F.1    Cavalli, G.2
  • 11
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modifications in DNA repair
    • Bergink S., Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature 2009, 458:461-467.
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 13
    • 0034754698 scopus 로고    scopus 로고
    • Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae
    • Biggins S., Bhalla N., Chang A., Smith D.L., Murray A.W. Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae. Genetics 2001, 159:453-470.
    • (2001) Genetics , vol.159 , pp. 453-470
    • Biggins, S.1    Bhalla, N.2    Chang, A.3    Smith, D.L.4    Murray, A.W.5
  • 14
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • Bird A. DNA methylation patterns and epigenetic memory. Genes Dev. 2002, 16:6-21.
    • (2002) Genes Dev. , vol.16 , pp. 6-21
    • Bird, A.1
  • 15
    • 33947317206 scopus 로고    scopus 로고
    • The epigenetic regulation of mammalian telomeres
    • Blasco M.A. The epigenetic regulation of mammalian telomeres. Nat. Rev. Genet. 2007, 8:299-309.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 299-309
    • Blasco, M.A.1
  • 16
    • 69249220176 scopus 로고    scopus 로고
    • DNA methylation and methyl-CpG binding proteins: developmental requirements and function
    • Bogdanović O., Veenstra G.J. DNA methylation and methyl-CpG binding proteins: developmental requirements and function. Chromosoma 2009, 118:549-565.
    • (2009) Chromosoma , vol.118 , pp. 549-565
    • Bogdanović, O.1    Veenstra, G.J.2
  • 18
    • 33750437743 scopus 로고    scopus 로고
    • Ubc9- and mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks
    • Branzei D., Sollier J., Liberi G., Zhao X., Maeda D., Seki M., Enomoto T., Ohta K., Foiani M. Ubc9- and mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks. Cell 2006, 127:509-522.
    • (2006) Cell , vol.127 , pp. 509-522
    • Branzei, D.1    Sollier, J.2    Liberi, G.3    Zhao, X.4    Maeda, D.5    Seki, M.6    Enomoto, T.7    Ohta, K.8    Foiani, M.9
  • 19
    • 56749132295 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO)-1, SUMO-2/3 and SUMOylation are involved with centromeric heterochromatin of chromosomes 9 and 1 and proteins of the synaptonemal complex during meiosis in men
    • Brown P.W., Hwang K., Schlegel P.N., Morris P.L. Small ubiquitin-related modifier (SUMO)-1, SUMO-2/3 and SUMOylation are involved with centromeric heterochromatin of chromosomes 9 and 1 and proteins of the synaptonemal complex during meiosis in men. Hum. Reprod. 2008, 23:2850-2857.
    • (2008) Hum. Reprod. , vol.23 , pp. 2850-2857
    • Brown, P.W.1    Hwang, K.2    Schlegel, P.N.3    Morris, P.L.4
  • 20
    • 33646584197 scopus 로고    scopus 로고
    • SUMO conjugation attenuates the activity of the gypsy chromatin insulator
    • Capelson M., Corces V.G. SUMO conjugation attenuates the activity of the gypsy chromatin insulator. EMBO J. 2006, 25:1906-1914.
    • (2006) EMBO J. , vol.25 , pp. 1906-1914
    • Capelson, M.1    Corces, V.G.2
  • 21
    • 84857198777 scopus 로고    scopus 로고
    • LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis
    • Castle C.D., Cassimere E.K., Denicourt C. LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis. Mol. Biol. Cell 2012, 23:716-728.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 716-728
    • Castle, C.D.1    Cassimere, E.K.2    Denicourt, C.3
  • 23
    • 35048872745 scopus 로고    scopus 로고
    • Topoisomerase I-dependent viability loss in saccharomyces cerevisiae mutants defective in both SUMO conjugation and DNA repair
    • Chen X.L., Silver H.R., Xiong L., Belichenko I., Adegite C., Johnson E.S. Topoisomerase I-dependent viability loss in saccharomyces cerevisiae mutants defective in both SUMO conjugation and DNA repair. Genetics 2007, 177:17-30.
    • (2007) Genetics , vol.177 , pp. 17-30
    • Chen, X.L.1    Silver, H.R.2    Xiong, L.3    Belichenko, I.4    Adegite, C.5    Johnson, E.S.6
  • 24
    • 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
  • 25
    • 81355161213 scopus 로고    scopus 로고
    • De novo assembly of a PML nuclear subcompartment occurs through multiple pathways and induces telomere elongation
    • Chung I., Leonhardt H., Rippe K. De novo assembly of a PML nuclear subcompartment occurs through multiple pathways and induces telomere elongation. J. Cell Sci. 2011, 124:3603-3618.
    • (2011) J. Cell Sci. , vol.124 , pp. 3603-3618
    • Chung, I.1    Leonhardt, H.2    Rippe, K.3
  • 26
    • 18144404319 scopus 로고    scopus 로고
    • A small conserved surface in SUMO is the critical structural determinant of its transcriptional inhibitory properties
    • Chupreta S., Holmstrom S., Subramanian L., Iñiguez-Lluhí J.A. A small conserved surface in SUMO is the critical structural determinant of its transcriptional inhibitory properties. Mol. Cell. Biol. 2005, 25:4272-4282.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4272-4282
    • Chupreta, S.1    Holmstrom, S.2    Subramanian, L.3    Iñiguez-Lluhí, J.A.4
  • 27
    • 84862783021 scopus 로고    scopus 로고
    • Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpoint
    • Cremona C.A., Sarangi P., Yang Y., Hang L.E., Rahman S., Zhao X. Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpoint. Mol. Cell 2012, 45:422-432.
    • (2012) Mol. Cell , vol.45 , pp. 422-432
    • Cremona, C.A.1    Sarangi, P.2    Yang, Y.3    Hang, L.E.4    Rahman, S.5    Zhao, X.6
  • 28
    • 38949174194 scopus 로고    scopus 로고
    • Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2
    • Darst R.P., Garcia S.N., Koch M.R., Pillus L. Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2. Mol. Cell. Biol. 2008, 28:1361-1372.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1361-1372
    • Darst, R.P.1    Garcia, S.N.2    Koch, M.R.3    Pillus, L.4
  • 29
    • 40749131181 scopus 로고    scopus 로고
    • Emerging roles of the SUMO pathway in mitosis
    • Dasso M. Emerging roles of the SUMO pathway in mitosis. Cell Div. 2008, 3:5.
    • (2008) Cell Div. , vol.3 , pp. 5
    • Dasso, M.1
  • 30
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • David G., Neptune M.A., DePinho R.A. SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J. Biol. Chem. 2002, 277:23658-23663.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    DePinho, R.A.3
  • 32
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: the protein complex that shapes and safeguards human telomeres
    • de Lange T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 2005, 19:2100-2110.
    • (2005) Genes Dev. , vol.19 , pp. 2100-2110
    • de Lange, T.1
  • 34
    • 33747329116 scopus 로고    scopus 로고
    • The modification of Sp3 isoforms by SUMOylation has differential effects on the SRC1A promoter
    • Ellis D.J., Dehm S.M., Bonham K. The modification of Sp3 isoforms by SUMOylation has differential effects on the SRC1A promoter. Gene 2006, 379:68-78.
    • (2006) Gene , vol.379 , pp. 68-78
    • Ellis, D.J.1    Dehm, S.M.2    Bonham, K.3
  • 36
    • 79960004074 scopus 로고    scopus 로고
    • The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast
    • Ferreira H.C., Luke B., Schober H., Kalck V., Lingner J., Gasser S.M. The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast. Nat. Cell Biol. 2011, 13:867-874.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 867-874
    • Ferreira, H.C.1    Luke, B.2    Schober, H.3    Kalck, V.4    Lingner, J.5    Gasser, S.M.6
  • 37
    • 79952756302 scopus 로고    scopus 로고
    • The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex
    • Finkbeiner E., Haindl M., Muller S. The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex. EMBO J. 2011, 30:1067-1078.
    • (2011) EMBO J. , vol.30 , pp. 1067-1078
    • Finkbeiner, E.1    Haindl, M.2    Muller, S.3
  • 39
    • 69249203574 scopus 로고    scopus 로고
    • SUMO association with repressor complexes, emerging routes for transcriptional control
    • Garcia-Dominguez M., Reyes J.C. SUMO association with repressor complexes, emerging routes for transcriptional control. Biochim. Biophys. Acta 2009, 1789:451-459.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 451-459
    • Garcia-Dominguez, M.1    Reyes, J.C.2
  • 40
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau J.R., Lima C.D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 2010, 11:861-871.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 42
    • 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
  • 45
    • 84863112760 scopus 로고    scopus 로고
    • SUMO conjugation is required for the assembly of Drosophila Su(Hw) and Mod(mdg4) into insulator bodies that facilitate insulator complex formation
    • Golovnin A., Volkov I., Georgiev P. SUMO conjugation is required for the assembly of Drosophila Su(Hw) and Mod(mdg4) into insulator bodies that facilitate insulator complex formation. J. Cell Sci. 2012, 125:2064-2074.
    • (2012) J. Cell Sci. , vol.125 , pp. 2064-2074
    • Golovnin, A.1    Volkov, I.2    Georgiev, P.3
  • 47
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • Gong L., Yeh E.T. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J. Biol. Chem. 2006, 281:15869-15877.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.2
  • 48
    • 79961029209 scopus 로고    scopus 로고
    • SUMOylation regulates telomere length homeostasis by targeting Cdc13
    • Hang L.E., Liu X., Cheung I., Yang Y., Zhao X. SUMOylation regulates telomere length homeostasis by targeting Cdc13. Nat. Struct. Mol. Biol. 2011, 18:920-926.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 920-926
    • Hang, L.E.1    Liu, X.2    Cheung, I.3    Yang, Y.4    Zhao, X.5
  • 49
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland U., Steinacher R., Jiricny J., Schär P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 2002, 21:1456-1464.
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schär, P.4
  • 50
    • 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 K.L., Cook K.R., Karpen G.H. The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family. Genes Dev. 2001, 15:1334-1348.
    • (2001) Genes Dev. , vol.15 , pp. 1334-1348
    • Hari, K.L.1    Cook, K.R.2    Karpen, G.H.3
  • 51
    • 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
  • 52
    • 15744399172 scopus 로고    scopus 로고
    • Centromeric chromatin: what makes it unique?
    • Henikoff S., Dalal Y. Centromeric chromatin: what makes it unique?. Curr. Opin. Genet. Dev. 2005, 15:177-184.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 177-184
    • Henikoff, S.1    Dalal, Y.2
  • 54
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson E.S. Protein modification by SUMO. Annu. Rev. Biochem. 2004, 73:355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 55
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • Joseph J., Liu S.T., Jablonski S.A., Yen T.J., Dasso M. The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr. Biol. 2004, 14:611-617.
    • (2004) Curr. Biol. , vol.14 , pp. 611-617
    • Joseph, J.1    Liu, S.T.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 56
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey M.H., Melhuish T.A., Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell 2003, 113:127-137.
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 57
    • 13244271351 scopus 로고    scopus 로고
    • Multiple activities contribute to Pc2 E3 function
    • Kagey M.H., Melhuish T.A., Powers S.E., Wotton D. Multiple activities contribute to Pc2 E3 function. EMBO J. 2005, 24:108-119.
    • (2005) EMBO J. , vol.24 , pp. 108-119
    • Kagey, M.H.1    Melhuish, T.A.2    Powers, S.E.3    Wotton, D.4
  • 58
    • 59649124496 scopus 로고    scopus 로고
    • Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break
    • Kalocsay M., Hiller N.J., Jentsch S. Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. Mol. Cell 2009, 33:335-343.
    • (2009) Mol. Cell , vol.33 , pp. 335-343
    • Kalocsay, M.1    Hiller, N.J.2    Jentsch, S.3
  • 59
    • 0035861938 scopus 로고    scopus 로고
    • Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1
    • Kang E.S., Park C.W., Chung J.H. Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1. Biochem. Biophys. Res. Commun. 2001, 289:862-868.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 862-868
    • Kang, E.S.1    Park, C.W.2    Chung, J.H.3
  • 60
    • 77950907937 scopus 로고    scopus 로고
    • SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development
    • Kang X., Qi Y., Zuo Y., Wang Q., Zou Y., Schwartz R.J., Cheng J., Yeh E.T.H. SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development. Mol. Cell 2010, 38:191-201.
    • (2010) Mol. Cell , vol.38 , pp. 191-201
    • Kang, X.1    Qi, Y.2    Zuo, Y.3    Wang, Q.4    Zou, Y.5    Schwartz, R.J.6    Cheng, J.7    Yeh, E.T.H.8
  • 61
    • 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
  • 63
    • 49049120998 scopus 로고    scopus 로고
    • Developmental control of sumoylation pathway proteins in mouse male germ cells
    • La Salle S., Sun F., Zhang X.D., Matunis M.J., Handel M.A. Developmental control of sumoylation pathway proteins in mouse male germ cells. Dev. Biol. 2008, 321:227-237.
    • (2008) Dev. Biol. , vol.321 , pp. 227-237
    • La Salle, S.1    Sun, F.2    Zhang, X.D.3    Matunis, M.J.4    Handel, M.A.5
  • 64
    • 69249241855 scopus 로고    scopus 로고
    • SUMOylation enhances DNA methyltransferase 1 activity
    • Lee B., Muller M.T. SUMOylation enhances DNA methyltransferase 1 activity. Biochem. J. 2009, 421:449-461.
    • (2009) Biochem. J. , vol.421 , pp. 449-461
    • Lee, B.1    Muller, M.T.2
  • 65
    • 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
  • 66
    • 79961242786 scopus 로고    scopus 로고
    • Eliminating SF-1 (NR5A1) sumoylation in vivo results in ectopic hedgehog signaling and disruption of endocrine development
    • Lee F.Y., Faivre E.J., Suzawa M., Lontok E., Ebert D., Cai F., Belsham D.D., Ingraham H.A. Eliminating SF-1 (NR5A1) sumoylation in vivo results in ectopic hedgehog signaling and disruption of endocrine development. Dev. Cell 2011, 21:315-327.
    • (2011) Dev. Cell , vol.21 , pp. 315-327
    • Lee, F.Y.1    Faivre, E.J.2    Suzawa, M.3    Lontok, E.4    Ebert, D.5    Cai, F.6    Belsham, D.D.7    Ingraham, H.A.8
  • 67
    • 0033977682 scopus 로고    scopus 로고
    • Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies
    • Lehembre F., Badenhorst P., Müller S., Travers A., Schweisguth F., Dejean A. Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies. Mol. Cell. Biol. 2000, 20:1072-1082.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1072-1082
    • Lehembre, F.1    Badenhorst, P.2    Müller, S.3    Travers, A.4    Schweisguth, F.5    Dejean, A.6
  • 68
    • 34447127473 scopus 로고    scopus 로고
    • Polycomb protein Cbx4 promotes SUMO modification of de novo DNA methyltransferase Dnmt3a
    • Li B., Zhou J., Liu P., Hu J., Jin H., Shimono Y., Takahashi M., Xu G. Polycomb protein Cbx4 promotes SUMO modification of de novo DNA methyltransferase Dnmt3a. Biochem. J. 2007, 405:369-378.
    • (2007) Biochem. J. , vol.405 , pp. 369-378
    • Li, B.1    Zhou, J.2    Liu, P.3    Hu, J.4    Jin, H.5    Shimono, Y.6    Takahashi, M.7    Xu, G.8
  • 69
    • 1342306395 scopus 로고    scopus 로고
    • Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription
    • Ling Y., Sankpal U.T., Robertson A.K., McNally J.G., Karpova T., Robertson K.D. Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription. Nucleic Acids Res. 2004, 32:598-610.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 598-610
    • Ling, Y.1    Sankpal, U.T.2    Robertson, A.K.3    McNally, J.G.4    Karpova, T.5    Robertson, K.D.6
  • 70
    • 2942630097 scopus 로고    scopus 로고
    • Encoded errors: mutations and rearrangements mediated by misalignment at repetitive DNA sequences
    • Lovett S.T. Encoded errors: mutations and rearrangements mediated by misalignment at repetitive DNA sequences. Mol. Microbiol. 2004, 52:1243-1253.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1243-1253
    • Lovett, S.T.1
  • 71
    • 77449147101 scopus 로고    scopus 로고
    • Sumoylation of the BLM ortholog, Sgs1, promotes telomere-telomere recombination in budding yeast
    • Lu C.Y., Tsai C.H., Brill S.J., Teng S.C. Sumoylation of the BLM ortholog, Sgs1, promotes telomere-telomere recombination in budding yeast. Nucleic Acids Res. 2010, 38:488-498.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 488-498
    • Lu, C.Y.1    Tsai, C.H.2    Brill, S.J.3    Teng, S.C.4
  • 72
    • 33751099563 scopus 로고    scopus 로고
    • Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins
    • Lyst M.J., Nan X., Stancheva I. Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins. EMBO J. 2006, 25:5317-5328.
    • (2006) EMBO J. , vol.25 , pp. 5317-5328
    • Lyst, M.J.1    Nan, X.2    Stancheva, I.3
  • 75
    • 84861323247 scopus 로고    scopus 로고
    • The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin
    • Maison C., Romeo K., Bailly D., Dubarry M., Quivy J.P., Almouzni G. The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin. Nat. Struct. Mol. Biol. 2012, 19:458-460.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 458-460
    • Maison, C.1    Romeo, K.2    Bailly, D.3    Dubarry, M.4    Quivy, J.P.5    Almouzni, G.6
  • 78
    • 71049147061 scopus 로고    scopus 로고
    • Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition
    • Matafora V., D'Amato A., Mori S., Blasi F., Bachi A. Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition. Mol. Cell. Proteomics 2009, 8:2243-2255.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2243-2255
    • Matafora, V.1    D'Amato, A.2    Mori, S.3    Blasi, F.4    Bachi, A.5
  • 80
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh P.B., Koshland D. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 1995, 6:793-807.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 83
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: the SUMO proteases
    • Mukhopadhyay D., Dasso M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 2007, 32:286-295.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 84
    • 77949378117 scopus 로고    scopus 로고
    • The SUMO protease SENP6 is essential for inner kinetochore assembly
    • Mukhopadhyay D., Arnaoutov A., Dasso M. The SUMO protease SENP6 is essential for inner kinetochore assembly. J. Cell Biol. 2010, 188:681-692.
    • (2010) J. Cell Biol. , vol.188 , pp. 681-692
    • Mukhopadhyay, D.1    Arnaoutov, A.2    Dasso, M.3
  • 85
    • 77955286868 scopus 로고    scopus 로고
    • Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the Slx5-Slx8 SUMO-targeted ubiquitin ligase
    • Mullen J.R., Chen C.F., Brill S.J. Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the Slx5-Slx8 SUMO-targeted ubiquitin ligase. Mol. Cell. Biol. 2010, 30:3737-3748.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3737-3748
    • Mullen, J.R.1    Chen, C.F.2    Brill, S.J.3
  • 88
    • 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
  • 90
    • 33845286542 scopus 로고    scopus 로고
    • BRCA1 foci in normal S-phase nuclei are linked to interphase centromeres and replication of pericentric heterochromatin
    • Pageau G.J., Lawrence J.B. BRCA1 foci in normal S-phase nuclei are linked to interphase centromeres and replication of pericentric heterochromatin. J. Cell Biol. 2006, 175:693-701.
    • (2006) J. Cell Biol. , vol.175 , pp. 693-701
    • Pageau, G.J.1    Lawrence, J.B.2
  • 91
    • 33748574525 scopus 로고    scopus 로고
    • Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway
    • Panse V.G., Kressler D., Pauli A., Petfalski E., Gnädig M., Tollervey D., Hurt E. Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway. Traffic 2006, 7:1311-1321.
    • (2006) Traffic , vol.7 , pp. 1311-1321
    • Panse, V.G.1    Kressler, D.2    Pauli, A.3    Petfalski, E.4    Gnädig, M.5    Tollervey, D.6    Hurt, E.7
  • 92
    • 84859133897 scopus 로고    scopus 로고
    • The SUMO E3 ligase Siz2 exerts a locus dependent effect on gene silencing in Saccharomyces cerevisiae
    • Pasupala N., Easwaran S., Hannan A., Shore D., Mishra K. The SUMO E3 ligase Siz2 exerts a locus dependent effect on gene silencing in Saccharomyces cerevisiae. Eukaryot. Cell 2012, 11:452-462.
    • (2012) Eukaryot. Cell , vol.11 , pp. 452-462
    • Pasupala, N.1    Easwaran, S.2    Hannan, A.3    Shore, D.4    Mishra, K.5
  • 93
    • 56549108671 scopus 로고    scopus 로고
    • Localization of Smc5/6 to centromeres and telomeres requires heterochromatin and SUMO, respectively
    • Pebernard S., Schaffer L., Campbell D., Head S.R., Boddy M.N. Localization of Smc5/6 to centromeres and telomeres requires heterochromatin and SUMO, respectively. EMBO J. 2008, 27:3011-3023.
    • (2008) EMBO J. , vol.27 , pp. 3011-3023
    • Pebernard, S.1    Schaffer, L.2    Campbell, D.3    Head, S.R.4    Boddy, M.N.5
  • 95
    • 34447129654 scopus 로고    scopus 로고
    • The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins
    • Potts P.R., Yu H. The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nat. Struct. Mol. Biol. 2007, 14:581-590.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 581-590
    • Potts, P.R.1    Yu, H.2
  • 96
    • 23044477079 scopus 로고    scopus 로고
    • Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans
    • Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J. Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans. EMBO J. 2005, 24:2613-2623.
    • (2005) EMBO J. , vol.24 , pp. 2613-2623
    • Poulin, G.1    Dong, Y.2    Fraser, A.G.3    Hopper, N.A.4    Ahringer, J.5
  • 97
    • 50549091334 scopus 로고    scopus 로고
    • The polycomb repressive complex 2 is a potential target of SUMO modifications
    • Riising E.M., Boggio R., Chiocca S., Helin K., Pasini D. The polycomb repressive complex 2 is a potential target of SUMO modifications. PLoS ONE 2008, 3:e2704.
    • (2008) PLoS ONE , vol.3
    • Riising, E.M.1    Boggio, R.2    Chiocca, S.3    Helin, K.4    Pasini, D.5
  • 98
    • 7744223823 scopus 로고    scopus 로고
    • SUMO modified proteins localize to the XY body of pachytene spermatocytes
    • Rogers R.S., Inselman A., Handel M.A., Matunis M.J. SUMO modified proteins localize to the XY body of pachytene spermatocytes. Chromosoma 2004, 113:233-243.
    • (2004) Chromosoma , vol.113 , pp. 233-243
    • Rogers, R.S.1    Inselman, A.2    Handel, M.A.3    Matunis, M.J.4
  • 99
    • 77953929082 scopus 로고    scopus 로고
    • SUMO functions in constitutive transcription and during activation of inducible genes in yeast
    • Rosonina E., Duncan S.M., Manley J.L. SUMO functions in constitutive transcription and during activation of inducible genes in yeast. Genes Dev. 2010, 24:1242-1252.
    • (2010) Genes Dev. , vol.24 , pp. 1242-1252
    • Rosonina, E.1    Duncan, S.M.2    Manley, J.L.3
  • 100
    • 84857176030 scopus 로고    scopus 로고
    • Sumoylation of transcription factor Gcn4 facilitates its Srb10-mediated clearance from promoters in yeast
    • Rosonina E., Duncan S.M., Manley J.L. Sumoylation of transcription factor Gcn4 facilitates its Srb10-mediated clearance from promoters in yeast. Genes Dev. 2012, 26:350-355.
    • (2012) Genes Dev. , vol.26 , pp. 350-355
    • Rosonina, E.1    Duncan, S.M.2    Manley, J.L.3
  • 101
    • 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 2002, 10:831-842.
    • (2002) Mol. Cell , vol.10 , pp. 831-842
    • Ross, S.1    Best, J.L.2    Zon, L.I.3    Gill, G.4
  • 102
    • 77957770103 scopus 로고    scopus 로고
    • Rod/Zw10 complex is required for PIASy-dependent centromeric SUMOylation
    • Ryu H., Azuma Y. Rod/Zw10 complex is required for PIASy-dependent centromeric SUMOylation. J. Biol. Chem. 2010, 285:32576-32585.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32576-32585
    • Ryu, H.1    Azuma, Y.2
  • 103
    • 4744375522 scopus 로고    scopus 로고
    • Complexity of translationally controlled transcription factor Sp3 isoform expression
    • Sapetschnig A., Koch F., Rischitor G., Mennenga T., Suske G. Complexity of translationally controlled transcription factor Sp3 isoform expression. J. Biol. Chem. 2004, 279:42095-42105.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42095-42105
    • Sapetschnig, A.1    Koch, F.2    Rischitor, G.3    Mennenga, T.4    Suske, G.5
  • 105
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert W., Futcher B., Jentsch S. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 1995, 373:78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 107
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio Y., Eisenman R.N. Histone sumoylation is associated with transcriptional repression. Proc. Natl. Acad. Sci. USA 2003, 100:13225-13230.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13225-13230
    • Shiio, Y.1    Eisenman, R.N.2
  • 108
    • 24944528328 scopus 로고    scopus 로고
    • SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast
    • Shin J.A., Choi E.S., Kim H.S., Ho J.C., Watts F.Z., Park S.D., Jang Y.K. SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast. Mol. Cell 2005, 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    Park, S.D.6    Jang, Y.K.7
  • 110
    • 79953220519 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) conjugation impedes transcriptional silencing by the polycomb group repressor Sex Comb on Midleg
    • Smith M., Mallin D.R., Simon J.A., Courey A.J. Small ubiquitin-like modifier (SUMO) conjugation impedes transcriptional silencing by the polycomb group repressor Sex Comb on Midleg. J. Biol. Chem. 2011, 286:11391-11400.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11391-11400
    • Smith, M.1    Mallin, D.R.2    Simon, J.A.3    Courey, A.J.4
  • 111
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 138:389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 112
    • 79960911178 scopus 로고    scopus 로고
    • The UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression
    • Spektor T.M., Congdon L.M., Veerappan C.S., Rice J.C. The UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression. PLoS ONE 2011, 6:e22785.
    • (2011) PLoS ONE , vol.6
    • Spektor, T.M.1    Congdon, L.M.2    Veerappan, C.S.3    Rice, J.C.4
  • 113
    • 80052766372 scopus 로고    scopus 로고
    • The Nse2/Mms21 SUMO ligase of the Smc5/6 complex in the maintenance of genome stability
    • Stephan A.K., Kliszczak M., Morrison C.G. The Nse2/Mms21 SUMO ligase of the Smc5/6 complex in the maintenance of genome stability. FEBS Lett. 2011, 585:2907-2913.
    • (2011) FEBS Lett. , vol.585 , pp. 2907-2913
    • Stephan, A.K.1    Kliszczak, M.2    Morrison, C.G.3
  • 114
    • 40849150778 scopus 로고    scopus 로고
    • Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen
    • Stielow B., Sapetschnig A., Krüger 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    Krüger, I.3    Kunert, N.4    Brehm, A.5    Boutros, M.6    Suske, G.7
  • 115
    • 51049083598 scopus 로고    scopus 로고
    • SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing
    • Stielow B., Sapetschnig A., Wink C., Krüger I., Suske G. SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing. EMBO Rep. 2008, 9:899-906.
    • (2008) EMBO Rep. , vol.9 , pp. 899-906
    • Stielow, B.1    Sapetschnig, A.2    Wink, C.3    Krüger, I.4    Suske, G.5
  • 118
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka K., Nishide J., Okazaki K., Kato H., Niwa O., Nakagawa T., Matsuda H., Kawamukai M., Murakami Y. Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 1999, 19:8660-8672.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1    Nishide, J.2    Okazaki, K.3    Kato, H.4    Niwa, O.5    Nakagawa, T.6    Matsuda, H.7    Kawamukai, M.8    Murakami, Y.9
  • 122
    • 84863003858 scopus 로고    scopus 로고
    • An acetylation switch regulates SUMO-dependent protein interaction networks
    • Ullmann R., Chien C.D., Avantaggiati M.L., Muller S. An acetylation switch regulates SUMO-dependent protein interaction networks. Mol. Cell 2012, 46:759-770.
    • (2012) Mol. Cell , vol.46 , pp. 759-770
    • Ullmann, R.1    Chien, C.D.2    Avantaggiati, M.L.3    Muller, S.4
  • 123
    • 62549158636 scopus 로고    scopus 로고
    • Sumoylation precedes accumulation of phosphorylated H2AX on sex chromosomes during their meiotic inactivation
    • Vigodner M. Sumoylation precedes accumulation of phosphorylated H2AX on sex chromosomes during their meiotic inactivation. Chromosome Res. 2009, 17:37-45.
    • (2009) Chromosome Res. , vol.17 , pp. 37-45
    • Vigodner, M.1
  • 124
    • 33646428383 scopus 로고    scopus 로고
    • SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis
    • Vigodner M., Ishikawa T., Schlegel P.N., Morris P.L. SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis. Am. J. Physiol. Endocrinol. Metab. 2006, 290:E1022-E1033.
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.290
    • Vigodner, M.1    Ishikawa, T.2    Schlegel, P.N.3    Morris, P.L.4
  • 126
    • 77955990555 scopus 로고    scopus 로고
    • A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58
    • Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E., Lamond A.I. A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58. Mol. Cell 2010, 39:618-631.
    • (2010) Mol. Cell , vol.39 , pp. 618-631
    • Westman, B.J.1    Verheggen, C.2    Hutten, S.3    Lam, Y.W.4    Bertrand, E.5    Lamond, A.I.6
  • 127
    • 77956095231 scopus 로고    scopus 로고
    • Active DNA demethylation: many roads lead to Rome
    • Wu S.C., Zhang Y. Active DNA demethylation: many roads lead to Rome. Nat. Rev. Mol. Cell Biol. 2010, 11:607-620.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 607-620
    • Wu, S.C.1    Zhang, Y.2
  • 128
    • 6344254386 scopus 로고    scopus 로고
    • Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance
    • Xhemalce B., Seeler J.S., Thon G., Dejean A., Arcangioli B. Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance. EMBO J. 2004, 23:3844-3853.
    • (2004) EMBO J. , vol.23 , pp. 3844-3853
    • Xhemalce, B.1    Seeler, J.S.2    Thon, G.3    Dejean, A.4    Arcangioli, B.5
  • 130
    • 1542285164 scopus 로고    scopus 로고
    • SUMO promotes HDAC-mediated transcriptional repression
    • Yang S.H., Sharrocks A.D. SUMO promotes HDAC-mediated transcriptional repression. Mol. Cell 2004, 13:611-617.
    • (2004) Mol. Cell , vol.13 , pp. 611-617
    • Yang, S.H.1    Sharrocks, A.D.2
  • 131
    • 79955841523 scopus 로고    scopus 로고
    • Inhibition of androgen receptor activity by histone deacetylase 4 through receptor SUMOylation
    • Yang Y., Tse A.K.-W., Li P., Ma Q., Xiang S., Nicosia S.V., Seto E., Zhang X., Bai W. Inhibition of androgen receptor activity by histone deacetylase 4 through receptor SUMOylation. Oncogene 2011, 30:2207-2218.
    • (2011) Oncogene , vol.30 , pp. 2207-2218
    • Yang, Y.1    Tse, A.K.-W.2    Li, P.3    Ma, Q.4    Xiang, S.5    Nicosia, S.V.6    Seto, E.7    Zhang, X.8    Bai, W.9
  • 132
  • 133
    • 2442439113 scopus 로고    scopus 로고
    • SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2
    • Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S., Haber D.A. SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2. Nat. Genet. 2004, 36:507-511.
    • (2004) Nat. Genet. , vol.36 , pp. 507-511
    • Zhang, H.1    Smolen, G.A.2    Palmer, R.3    Christoforou, A.4    van den Heuvel, S.5    Haber, D.A.6
  • 134
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang X.D., Goeres J., Zhang H., Yen T.J., Porter A.C., Matunis M.J. SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol. Cell 2008, 29:729-741.
    • (2008) Mol. Cell , vol.29 , pp. 729-741
    • Zhang, X.D.1    Goeres, J.2    Zhang, H.3    Yen, T.J.4    Porter, A.C.5    Matunis, M.J.6
  • 135
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao X., Blobel G. A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl. Acad. Sci. USA 2005, 102:4777-4782.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2
  • 136
    • 25444462980 scopus 로고    scopus 로고
    • Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications
    • Zhao X., Sternsdorf T., Bolger T.A., Evans R.M., Yao T.-P. Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications. Mol. Cell. Biol. 2005, 25:8456-8464.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8456-8464
    • Zhao, X.1    Sternsdorf, T.2    Bolger, T.A.3    Evans, R.M.4    Yao, T.-P.5


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