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Identification of SUMO sites by LC-MSMS

ABSTRACT: We developed a novel method for the identification of SUMO sites by expression of His-tagged SUMO mutants and affinity purification of SUMOylated proteins, followed by trypsin digestion and immunocapture of peptides containing diglycine signature tags. Lab Head: Dr Pascale Cossart, pascale.cossart@pasteur.fr Institut Pasteur Unité des Interactions Bactéries-Cellules, Inserm U604, INRA USC2020 25 rue du Dr. Roux 75015 Paris France

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Francis Impens

LAB HEAD: Francis Impens

PROVIDER: PXD000459 | Pride | 2014-07-29

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20130531_FI_SUMO1.raw	Raw
	20130531_FI_SUMO2.raw	Raw
	F008291.dat	Other
	F008293.dat	Other
	F008295.dat	Other

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Publications

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

Impens Francis F Radoshevich Lilliana L Cossart Pascale P Ribet David D

Proceedings of the National Academy of Sciences of the United States of America 20140811 34

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 st ...[more]

PMID: 25114211

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Quantitative K-GG site analysis

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2016-01-13 | PXD002408 | Pride

SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage

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