Something about SUMO inhibits transcription

Current Opinion in Genetics and Development

Volumn 15, Issue 5 SPEC. ISS., 2005, Pages 536-541

  Gill, Grace ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; REPRESSOR PROTEIN; SUMO PROTEIN; TRANSCRIPTION FACTOR;

ACETYLATION; BINDING SITE; COMPLEX FORMATION; ENZYME SUBSTRATE; GENE CONTROL; GENE EXPRESSION REGULATION; GENE REPRESSION; GENETIC TRANSCRIPTION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; REVIEW; TRANSCRIPTION REGULATION;

EID: 24344445216     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2005.07.004     Document Type: Review

References (50)

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25. ••], this study supports a role for HDACs as effectors of SUMO-dependent transcriptional repression.
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32. •], suggest that Daxx has properties consistent with those of a SUMO-dependent co-repressor.
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39. ••]. The authors show that SIRT1 deacetylates the SUMO-acceptor lysines in p300 CRD1. These studies support the model that the HDAC SIRT1 promotes SUMOylation of p300 by regulating accessibility of key lysine residues.
40. S. Gregoire, and X.J. Yang Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors Mol Cell Biol 25 2005 2273 2287 In their study, the authors demonstrate that post-translational modification of the MEF2C and MEF2D transcription factors by SUMO inhibits activation. When HDAC4 was co-expressed with MEF2 and SUMO, enhanced SUMOylation of MEF2 was observed. Enhanced SUMOylation of MEF2 required the MEF2-binding domain, but not the deacetylase domain of HDAC4. This non-enzymatic activity of HDAC4 was further increased by mutation of the SUMO-acceptor lysine in HDAC4.
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50. S. Chupreta, S. Holmstrom, L. Subramanian, and J.A. Iniguez-Lluhi A small conserved surface in SUMO is the critical structural determinant of its transcriptional inhibitory properties Mol Cell Biol 25 2005 4272 4282 In this study, the authors carry out a systematic mutational analysis to identify surface residues of SUMO-2 that are important for its function in inhibitionT of transcription. They identify a surface on SUMO, characterized by key hydrophobic and basic residues, that is important for repression in several contexts but which is not required for SUMO conjugation or deconjugation. This study defines a surface on SUMO that likely contributes to functional interactions with co-repressors bearing SUMO binding domains.