Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 2015 Sep 1;112(35):E4854-63. doi: 10.1073/pnas.1509716112. Epub 2015 Aug 17.

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

Author information

1
Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom;
2
Centre for Gene Regulation and Expression, University of Dundee, Dundee DD1 5EH, United Kingdom.
3
Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom; a.d.sharrocks@manchester.ac.uk.

Abstract

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.

KEYWORDS:

SIM; SUMO; ZMYM2; ZNF198; chromatin

PMID:
26283374
PMCID:
PMC4568223
DOI:
10.1073/pnas.1509716112
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center