Screen for multi-SUMO–binding proteins reveals a multi-SIM–binding mechanism for recruitment of the transcriptional regulator ZMYM2 to chromatin

Protein SUMOylation has emerged as an important regulatory event, particularly in nuclear processes such as transcriptional control and DNA repair. In this context, small ubiquitin-like modifier (SUMO) often provides a binding platform for the recruitment of proteins via their SUMO-interacting motif...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2015-09, Vol.112 (35), p.E4854-E4863
Main Authors: Aguilar-Martinez, Elisa, Chen, Xi, Webber, Aaron, Mould, A. Paul, Seifert, Anne, Hay, Ronald T., Sharrocks, Andrew D.
Format: Article
Language:English
Subjects:
Binding sites
Biological Sciences
Chromatin
Chromatin - metabolism
DNA repair
DNA-Binding Proteins - metabolism
HEK293 Cells
Humans
PNAS Plus
Protein Binding
Proteins
Small Ubiquitin-Related Modifier Proteins - metabolism
Transcription factors
Transcription Factors - metabolism
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Summary:Protein SUMOylation has emerged as an important regulatory event, particularly in nuclear processes such as transcriptional control and DNA repair. In this context, small ubiquitin-like modifier (SUMO) often provides a binding platform for the recruitment of proteins via their SUMO-interacting motifs (SIMs). Recent discoveries point to an important role for multivalent SUMO binding through multiple SIMs in the binding partner as exemplified by poly-SUMOylation acting as a binding platform for ubiquitin E3 ligases such as ring finger protein 4. Here, we have investigated whether other types of protein are recruited through multivalent SUMO interactions. We have identified dozens of proteins that bind to multi-SUMO platforms, thereby uncovering a complex potential regulatory network. Multi-SUMO binding is mediated through multi-SIM modules, and the functional importance of these interactions is demonstrated for the transcriptional corepressor ZMYM2/ZNF198 where its multi-SUMO–binding activity is required for its recruitment to chromatin.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1509716112