MAPKAP Kinase-2 phosphorylation of PABPC1 controls its interaction with 14-3-3 proteins after DNA damage: A combined kinase and protein array approach.
14-3-3
DNA damage
MAPKAP Kinase-2
polyA-binding protein
signal transduction
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2023
2023
Historique:
received:
20
01
2023
accepted:
23
03
2023
medline:
24
4
2023
pubmed:
24
4
2023
entrez:
24
04
2023
Statut:
epublish
Résumé
14-3-3 proteins play critical roles in controlling multiple aspects of the cellular response to stress and DNA damage including regulation of metabolism, cell cycle progression, cell migration, and apoptotic cell death by binding to protein substrates of basophilic protein kinases following their phosphorylation on specific serine/threonine residues. Although over 200 mammalian proteins that bind to 14-3-3 have been identified, largely through proteomic studies, in many cases the relevant protein kinase responsible for conferring 14-3-3-binding to these proteins is not known. To facilitate the identification of kinase-specific 14-3-3 clients, we developed a biochemical approach using high-density protein filter arrays and identified the translational regulatory molecule PABPC1 as a substrate for Chk1 and MAPKAP Kinase-2 (MK2)
Identifiants
pubmed: 37091863
doi: 10.3389/fmolb.2023.1148933
pii: 1148933
pmc: PMC10117672
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1148933Informations de copyright
Copyright © 2023 Stehn, Floyd, Wilker, Reinhardt, Clarke, Huang, Polakiewicz, Sonenberg, Kong and Yaffe.
Déclaration de conflit d'intérêts
RP was employed by Cell Signaling Technology. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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