In-Depth Characterization of the Staphylococcus aureus Phosphoproteome Reveals New Targets of Stk1.
Microbiology
bacteria
mass spectrometry
pathogens
phosphatases
phosphorylation
serine/threonine kinases
substrate identification
Journal
Molecular & cellular proteomics : MCP
ISSN: 1535-9484
Titre abrégé: Mol Cell Proteomics
Pays: United States
ID NLM: 101125647
Informations de publication
Date de publication:
2021
2021
Historique:
received:
17
07
2020
revised:
02
12
2020
accepted:
10
12
2020
pubmed:
15
1
2021
medline:
15
3
2022
entrez:
14
1
2021
Statut:
ppublish
Résumé
Staphylococcus aureus is a major cause of infections worldwide, and infection results in a variety of diseases. As of no surprise, protein phosphorylation is an important game player in signaling cascades and has been shown to be involved in S. aureus virulence. Albeit long neglected, eukaryotic-type serine/threonine kinases in S. aureus have been implicated in this complex signaling cascades. Due to the substoichiometric nature of protein phosphorylation and a lack of suitable analysis tools, the knowledge of these cascades is, however, to date, still limited. Here, were apply an optimized protocol for efficient phosphopeptide enrichment via Fe
Identifiants
pubmed: 33444734
pii: S1535-9476(20)35148-3
doi: 10.1074/mcp.RA120.002232
pmc: PMC7950182
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Phosphopeptides
0
Phosphoproteins
0
Proteome
0
Protein Kinases
EC 2.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100034Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare no competing financial interest.