Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.
PTM
TPST
fragmentation
heparan-sulfate 6-O-sulfotransferase
mass spectrometry
neutral loss
phosphorylation
secretome
sulfation
tyrosyl protein sulfotransferases
Journal
Journal of proteome research
ISSN: 1535-3907
Titre abrégé: J Proteome Res
Pays: United States
ID NLM: 101128775
Informations de publication
Date de publication:
01 12 2023
01 12 2023
Historique:
medline:
4
12
2023
pubmed:
8
11
2023
entrez:
8
11
2023
Statut:
ppublish
Résumé
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalyzed by Golgi-resident tyrosyl protein sulfo transferases (TPSTs). Information on sY in humans is currently limited to ∼50 proteins, with only a handful having verified sites of sulfation. As such, the contribution of sulfation to the regulation of biological processes remains poorly defined. Mass spectrometry (MS)-based proteomics is the method of choice for PTM analysis but has yet to be applied for systematic investigation of the "sulfome", primarily due to issues associated with discrimination of sY-containing from phosphotyrosine (pY)-containing peptides. In this study, we developed an MS-based workflow for sY-peptide characterization, incorporating optimized Zr
Identifiants
pubmed: 37939282
doi: 10.1021/acs.jproteome.3c00425
pmc: PMC10696596
doi:
Substances chimiques
Phosphopeptides
0
tyrosine O-sulfate
29166358BF
Tyrosine
42HK56048U
Proteins
0
Phosphotyrosine
21820-51-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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