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Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14.

Uncovering global SUMOylation signaling networks in a site-specific manner.

Author information

1
Department of Molecular Cell Biology, Leiden University Medical Center, Leiden, the Netherlands.
2
Department of Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.

Abstract

SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution MS, we have studied global SUMOylation in human cells in a site-specific manner, identifying a total of >4,300 SUMOylation sites in >1,600 proteins. To our knowledge, this is the first time that >1,000 SUMOylation sites have been identified under standard growth conditions. We quantitatively studied SUMOylation dynamics in response to SUMO protease inhibition, proteasome inhibition and heat shock. Many SUMOylated lysines have previously been reported to be ubiquitinated, acetylated or methylated, thus indicating cross-talk between SUMO and other post-translational modifications. We identified 70 phosphorylation and four acetylation events in proximity to SUMOylation sites, and we provide evidence for acetylation-dependent SUMOylation of endogenous histone H3. SUMOylation regulates target proteins involved in all nuclear processes including transcription, DNA repair, chromatin remodeling, precursor-mRNA splicing and ribosome assembly.

PMID:
25218447
PMCID:
PMC4259010
DOI:
10.1038/nsmb.2890
[Indexed for MEDLINE]
Free PMC Article
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