期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 34, 页码 12432-12437出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1413825111
关键词
posttranslational modification; Listeria; cortactin; actin; anillin
资金
- Institut Pasteur, Institut National de la Sante et de la Recherche Medicale (INSERM)
- Institut National de la Recherche Agronomique (INRA)
- Agence Nationale de Recherches (ERANET Pathogenomics LISTRESS)
- French Government's Investissement d'Avenir program, Laboratoire d'Excellence Integrative Biology of Emerging Infectious Diseases [ANR-10-LABX-62-IBEID]
- European Research Council (ERC) [233348 MODELIST]
- Fondation le Roch les Mousquetaires
- Fondation Louis-Jeantet
- Pasteur-Roux Fellowship
- Human Frontiers Science Program
- Senior International Research Scholar of the Howard Hughes Medical Institute
- INSERM Research Associate
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 tomapSUMOylation 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 SUMOylationmachinery, 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.
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