Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9.
Détails
Etat: Public
Version: Final published version
Licence: CC BY 4.0
ID Serval
serval:BIB_4D0914B0B753
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9.
Périodique
Molecular & cellular proteomics
ISSN
1535-9484 (Electronic)
ISSN-L
1535-9476
Statut éditorial
Publié
Date de publication
04/2020
Peer-reviewed
Oui
Volume
19
Numéro
4
Pages
655-671
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Publication Status: ppublish
Résumé
Protein phosphorylation cascades play a central role in the regulation of cell growth and protein kinases PKA, Sch9 and Ypk1 take center stage in regulating this process in S. cerevisiae To understand how these kinases co-ordinately regulate cellular functions we compared the phospho-proteome of exponentially growing cells without and with acute chemical inhibition of PKA, Sch9 and Ypk1. Sites hypo-phosphorylated upon PKA and Sch9 inhibition were preferentially located in RRxS/T-motifs suggesting that many are directly phosphorylated by these enzymes. Interestingly, when inhibiting Ypk1 we not only detected several hypo-phosphorylated sites in the previously reported RxRxxS/T-, but also in an RRxS/T-motif. Validation experiments revealed that neutral trehalase Nth1, a known PKA target, is additionally phosphorylated and activated downstream of Ypk1. Signaling through Ypk1 is therefore more closely related to PKA- and Sch9-signaling than previously appreciated and may perform functions previously only attributed to the latter kinases.
Mots-clé
AGC-kinases, Cell growth, Chemical genetics, Enzyme Inhibition*, Label-free quantification, Phosphoproteome, Protein Motifs*, Protein kinases*, Trehalase, Yeast*, Enzyme inhibition, cell growth, chemical genetics, label-free quantification, phosphoproteome, protein kinases, protein motifs, trehalase, yeast
Pubmed
Web of science
Open Access
Oui
Création de la notice
10/03/2020 15:29
Dernière modification de la notice
27/01/2021 8:08