Proteomics

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Identification of oxidized cysteine residues in signaling proteins in U937 cells at basal levels and upon diamide and hypochlorous acid stimulations.

ABSTRACT: Here, we report a detection of oxidative post-translational modifications (ox-PTM) of Cys residues in the U937 cell line either non-stimulated or stimulated with diamide, a thiol-oxidizing agent at 0.5mM for 20min or HOCl at 100µM for 10min. Reversible Cys ox-PTMs were labelled using a bioswitch method using a Maleimide-(Polyethylene Glycol)2-Biotin (Mal-PEG2-Bio) probe independently of the oxidation type. Labeled proteins were analyzed by Mass spectrometry. We identified Cys ox-PTMs encompassing 1473 proteins containing at least ox-PTM-modified Cys. These sites include ox-PTM sites previously described in vitro validating the approach. Numerous novel Cys susceptible to ox-PTMs were identified including signaling proteins, including kinases, phosphatases and transcription and translation factors and proteins relevant to virus-host interactions.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Monocyte

SUBMITTER: Nathalie Grandvaux  

LAB HEAD: Nathalie Grandvaux

PROVIDER: PXD020270 | Pride | 2023-03-10

REPOSITORIES: Pride

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Publications

Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs.

Cuervo Natalia Zamorano NZ   Grandvaux Nathalie N  

Redox biology 20221220

Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)-like domains harboring typical CXXC catalytic motifs responsible for redox reactions, as well as non-catalytic TRX-like domain. As increasing attention is paid to oxidative post-translational modifications of cysteines (Cys ox-PTMs) with the re  ...[more]

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