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Proc Natl Acad Sci U S A. 2014 Aug 26;111(34):12432-7. doi: 10.1073/pnas.1413825111. Epub 2014 Aug 11.

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

Author information

1
Unité des Interactions Bactéries-Cellules, Institut Pasteur, F-75015 Paris, France; Institut National de la Santé et de la Recherche Médicale, Unité 604, F-75015 Paris, France; and Institut National de la Recherche Agronomique, Unité sous-contrat 2020, F-75015 Paris, France.
2
Unité des Interactions Bactéries-Cellules, Institut Pasteur, F-75015 Paris, France; Institut National de la Santé et de la Recherche Médicale, Unité 604, F-75015 Paris, France; and Institut National de la Recherche Agronomique, Unité sous-contrat 2020, F-75015 Paris, France pcossart@pasteur.fr david.ribet@pasteur.fr.

Abstract

SUMOylation is an essential ubiquitin-like modification involved in important biological processes in eukaryotic cells. Identification of small ubiquitin-related modifier (SUMO)-conjugated residues in proteins is critical for understanding the role of SUMOylation but remains experimentally challenging. We have set up a powerful and high-throughput method combining quantitative proteomics and peptide immunocapture to map SUMOylation sites and have analyzed changes in SUMOylation in response to stimuli. With this technique we identified 295 SUMO1 and 167 SUMO2 sites on endogenous substrates of human cells. We further used this strategy to characterize changes in SUMOylation induced by listeriolysin O, a bacterial toxin that impairs the host cell SUMOylation machinery, and identified several classes of host proteins specifically deSUMOylated in response to this toxin. Our approach constitutes an unprecedented tool, broadly applicable to various SUMO-regulated cellular processes in health and disease.

KEYWORDS:

Listeria; actin; anillin; cortactin; posttranslational modification

PMID:
25114211
PMCID:
PMC4151716
DOI:
10.1073/pnas.1413825111
[Indexed for MEDLINE]
Free PMC Article
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