Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9.

Details

Serval ID
serval:BIB_4D0914B0B753
Type
Article: article from journal or magazin.
Collection
Publications
Title
Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9.
Journal
Molecular & cellular proteomics
Author(s)
Plank M., Perepelkina M., Müller M., Vaga S., Zou X., Bourgoint C., Berti M., Saarbach J., Haesendonckx S., Winssinger N., Aebersold R., Loewith R.
ISSN
1535-9484 (Electronic)
ISSN-L
1535-9476
Publication state
Published
Issued date
04/2020
Peer-reviewed
Oui
Volume
19
Number
4
Pages
655-671
Language
english
Notes
Publication types: Journal Article
Publication Status: ppublish
Abstract
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.
Keywords
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
Yes
Create date
10/03/2020 15:29
Last modification date
02/05/2020 18:32
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