SUMOylation of proteins involved in chromatin organization regulates gene expression in several ways: direct influence on catalytic activity of enzymes that modify chromatin, recruitment of proteins that form repressive (e.g. PRC1) or activating complexes on chromatin, recruitment of proteins to larger bodies (e.g PML bodies) in the nucleus (reviewed in Cubenas-Potts and Matunis 2013).
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Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET.; ''Characterization of a second member of the sentrin family of ubiquitin-like proteins.''; PubMedEurope PMCScholia
Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMedEurope PMCScholia
Brandl A, Wagner T, Uhlig KM, Knauer SK, Stauber RH, Melchior F, Schneider G, Heinzel T, Krämer OH.; ''Dynamically regulated sumoylation of HDAC2 controls p53 deacetylation and restricts apoptosis following genotoxic stress.''; PubMedEurope PMCScholia
Tan JA, Song J, Chen Y, Durrin LK.; ''Phosphorylation-dependent interaction of SATB1 and PIAS1 directs SUMO-regulated caspase cleavage of SATB1.''; PubMedEurope PMCScholia
Stielow C, Stielow B, Finkernagel F, Scharfe M, Jarek M, Suske G.; ''SUMOylation of the polycomb group protein L3MBTL2 facilitates repression of its target genes.''; PubMedEurope PMCScholia
Citro S, Jaffray E, Hay RT, Seiser C, Chiocca S.; ''A role for paralog-specific sumoylation in histone deacetylase 1 stability.''; PubMedEurope PMCScholia
Dobreva G, Dambacher J, Grosschedl R.; ''SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression.''; PubMedEurope PMCScholia
Ismail IH, Gagné JP, Caron MC, McDonald D, Xu Z, Masson JY, Poirier GG, Hendzel MJ.; ''CBX4-mediated SUMO modification regulates BMI1 recruitment at sites of DNA damage.''; PubMedEurope PMCScholia
Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMedEurope PMCScholia
Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMedEurope PMCScholia
Kabachinski G, Schwartz TU.; ''The nuclear pore complex--structure and function at a glance.''; PubMedEurope PMCScholia
Cheng J, Wang D, Wang Z, Yeh ET.; ''SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1.''; PubMedEurope PMCScholia
David G, Neptune MA, DePinho RA.; ''SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities.''; PubMedEurope PMCScholia
Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A.; ''Ubc9 sumoylation regulates SUMO target discrimination.''; PubMedEurope PMCScholia
Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A.; ''Architecture of the symmetric core of the nuclear pore.''; PubMedEurope PMCScholia
Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMedEurope PMCScholia
Tan JA, Sun Y, Song J, Chen Y, Krontiris TG, Durrin LK.; ''SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage.''; PubMedEurope PMCScholia
Riising EM, Boggio R, Chiocca S, Helin K, Pasini D.; ''The polycomb repressive complex 2 is a potential target of SUMO modifications.''; PubMedEurope PMCScholia
Merrill JC, Melhuish TA, Kagey MH, Yang SH, Sharrocks AD, Wotton D.; ''A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity.''; PubMedEurope PMCScholia
Roscic A, Möller A, Calzado MA, Renner F, Wimmer VC, Gresko E, Lüdi KS, Schmitz ML.; ''Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2.''; PubMedEurope PMCScholia
Lamoliatte F, Caron D, Durette C, Mahrouche L, Maroui MA, Caron-Lizotte O, Bonneil E, Chelbi-Alix MK, Thibault P.; ''Large-scale analysis of lysine SUMOylation by SUMO remnant immunoaffinity profiling.''; PubMedEurope PMCScholia
Kagey MH, Melhuish TA, Powers SE, Wotton D.; ''Multiple activities contribute to Pc2 E3 function.''; PubMedEurope PMCScholia
Tammsalu T, Matic I, Jaffray EG, Ibrahim AFM, Tatham MH, Hay RT.; ''Proteome-wide identification of SUMO2 modification sites.''; PubMedEurope PMCScholia
Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMedEurope PMCScholia
Kang X, Qi Y, Zuo Y, Wang Q, Zou Y, Schwartz RJ, Cheng J, Yeh ET.; ''SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development.''; PubMedEurope PMCScholia
Kirsh O, Seeler JS, Pichler A, Gast A, Müller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A.; ''The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.''; PubMedEurope PMCScholia
Shiio Y, Eisenman RN.; ''Histone sumoylation is associated with transcriptional repression.''; PubMedEurope PMCScholia
Cubeñas-Potts C, Matunis MJ.; ''SUMO: a multifaceted modifier of chromatin structure and function.''; PubMedEurope PMCScholia
Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMedEurope PMCScholia
Wagner T, Kiweler N, Wolff K, Knauer SK, Brandl A, Hemmerich P, Dannenberg JH, Heinzel T, Schneider G, Krämer OH.; ''Sumoylation of HDAC2 promotes NF-κB-dependent gene expression.''; PubMedEurope PMCScholia
Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenshuk H, Thibault P.; ''Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.''; PubMedEurope PMCScholia
Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMedEurope PMCScholia
Yamashita D, Moriuchi T, Osumi T, Hirose F.; ''Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2α.''; PubMedEurope PMCScholia
CBX4 SUMOylates BMI1 in Polycomb Repressive Complex 1 (PRC1) at lysine-88 (Ismail et al. 2012). SUMOylation of BMI1 is necessary for its accumulation at sites of DNA damage. CBX4 directly binds poly(ADP-ribose) synthesized by PARP1 at sites of damage.
CBX4 in Polycomb Repressive Complex 1 (PRC1) autoSUMOylates with SUMO1 (Kagey et al.2005, Roscic et al. 2006, Merrill et al. 2010). As inferred from mouse homologs, SUMOylation of CBX4 appears to be essential for recruitment of the PRC1 complex to histone H3 trimethylated at lysine-27 (H3K27me3) (Kang et al. 2010).
Histone H4 (HIST1H4) is SUMOylated at an unknown residue with SUMO3 (Shiio and Eisenman 2003). SUMOylation of histone H4 is associated with repression of transcription.
Histone H4 (HIST1H4) is SUMOylated at an unknown residue with SUMO1 (Shiio and Eisenman 2003). SUMOylated histone H4 is associated with repression of transcription.
PIAS1 SUMOylates SATB1 at lysine-744 with SUMO2,3 (Tan et al. 2008, Tan et al. 2010, Tammsalu et al. 2014). SUMOylation targets SATB1 to PML bodies where it is cleaved by caspase.
PIAS2-2 (PIASxbeta) SUMOylates SUZ12, a subunit of the Polycomb Repressive Complex 2 (PRC2), at lysine-75 with SUMO1 (Riising et al. 2008). SUMOyation does not affect the repression of transcription by PRC2. The effect of SUMOylation on PRC2 function is unknown. The EZH2 subunit of PRC2 can also be SUMOylated at multiple positions.
HDAC1 is SUMOylated at lysine-444 and lysine-476 with SUMO1 (Kirsh et al. 2002, David et al. 2002, Cheng et al. 2004, Citro et al. 2013). SUMOylation with SUMO1 enhances transcription repression by HDAC1 and promotes degradation of HDAC1 (Citro et al. 2013). HDAC1 can also be SUMOylated with SUMO2, which enhances stability of HDAC1 (Citro et al. 2013).
PIAS1 SUMOylates SATB2 at lysine-233 and lysine-350 with SUMO3 (Dobreva et al. 2003, Lamoliatte et al. 2013, Lamoliatte et al. 2014). SUMOylation reduces binding of SATB2 to matrix attachment regions and reduces activation of transcription by SATB2. SUMOylated SATB2 is localized to the nuclear periphery.
PIAS1 SUMOylates SATB1 at lysine-744 with SUMO1 (Tan et al. 2008, Tan et al. 2010). SUMOylation targets SATB1 to PML bodies where it is cleaved by caspase.
As inferred from mouse homologs, CBX5 (HP1 alpha) is SUMOylated at lysine-84 and other lysine residues with SUMO1. SUMOylated CBX5 associates with long non-coding transcripts in pericentric heterochromatin and SUMOylation is required for initial targeting of CBX5 to pericentric domains.
HDAC2 is SUMOylated at lysine-462 with SUMO1 (Brandl et al. 2012). SUMOylation of HDAC2 blocks TP53-dependent (p53-dependent) expression of genes but is required for induction of NF-kB-dependent gene expression (Wagner et al. 2015).
PIAS1 and possibly other SUMO E3 ligases SUMOylates L3MBTL2 with SUMO2 at lysine-675 and lysine-700 near the C-terminus (Stielow et al. 2014, Tammsalu et al. 2014). SUMOylation of L3MBTL2 does not appear to affect its chromatin binding activity, however SUMOylation does enhance transcriptional repression of a subset of L3MBTL2-target genes, particularly those with low L3MBTL2 occupancy including pro-inflammatory genes (Stielow et al. 2014). SUMOylated L3MBTL2 appears to increase the level of local ubiquitinated histone H2A (Stielow et al. 2014).
ZBED1 (hDREF) SUMOylates CHD3 (Mi2alpha) at lysine-1971 with SUMO1 (Yamashita et al. 2016). SUMOylation leads to dissociation of CHD3 from chromatin and suppresses transcriptional repression by CHD3.
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