Scientific article
Open access

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

Published inMolecular and Cellular Proteomics, vol. 19, no. 4, p. 655-671
Publication date2020

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.

  • Swiss National Science Foundation - SystemsX program (#51RTP0_151037)
Citation (ISO format)
PLANK, Michaël et al. Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9. In: Molecular and Cellular Proteomics, 2020, vol. 19, n° 4, p. 655–671. doi: 10.1074/mcp.RA120.001955
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Article (Published version)
ISSN of the journal1535-9476

Technical informations

Creation06/16/2020 11:15:00 AM
First validation06/16/2020 11:15:00 AM
Update time03/15/2023 10:07:16 PM
Status update03/15/2023 10:07:15 PM
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