Proceedings of the National Academy of Sciences - PNAS, 2014-08, Vol.111 (34), p.12432-12437
2014
Details
- Autor(en) / Beteiligte
- Titel
- Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli
- Ist Teil von
- Proceedings of the National Academy of Sciences - PNAS, 2014-08, Vol.111 (34), p.12432-12437
- Ort / Verlag
- United States: National Academy of Sciences
- Erscheinungsjahr
- 2014
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0027-8424eISSN: 1091-6490DOI: 10.1073/pnas.1413825111Titel-ID: cdi_pubmed_primary_25114211
- Format
- –
- Schlagworte
- Amino Acid Sequence, Amino acids, Antibodies, Bacterial Toxins - toxicity, Binding Sites, Biological Sciences, Cell culture techniques, Datasets, Enzymes, Eukaryotes, Heat-Shock Proteins - toxicity, HeLa Cells, Hemolysin Proteins - toxicity, Humans, Listeria, Molecular Sequence Data, Peptide Mapping - methods, Proteins, Proteomics, Proteomics - methods, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Recombinant Proteins - metabolism, Small Ubiquitin-Related Modifier Proteins - chemistry, Small Ubiquitin-Related Modifier Proteins - genetics, Small Ubiquitin-Related Modifier Proteins - metabolism, SUMO-1 Protein - chemistry, SUMO-1 Protein - genetics, SUMO-1 Protein - metabolism, Sumoylation - drug effects, Toxins, Ubiquitins