Proteomics

Dataset Information

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Multilayered control of protein turnover by TORC1 and ATG1


ABSTRACT: To study TORC1-Atg1 signaling comprehensively and to identify potential additional foci of crosstalk, we chose a mass spectrometry (MS)-based phosphoproteomics strategy combing global proteomics screens in vivo with targeted analyses using in vitro kinase reactions. We present the currently largest compendium of rapamycin-sensitive phosphorylation events in the yeast Saccharomyces cerevisiae, identify numerous unknown TORC1 and Atg1 downstream phosphorylation events, and characterize hitherto unknown, functionally relevant TORC1 target sites on defined Atg proteins.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Joern Dengjel  

LAB HEAD: Joern Dengjel

PROVIDER: PXD013271 | Pride | 2019-09-30

REPOSITORIES: Pride

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Publications


The target of rapamycin complex 1 (TORC1) is a master regulator of cell homeostasis, which promotes anabolic reactions and synchronously inhibits catabolic processes such as autophagy-mediated protein degradation. Its prime autophagy target is Atg13, a subunit of the Atg1 kinase complex that acts as the gatekeeper of canonical autophagy. To study whether the activities of TORC1 and Atg1 are coupled through additional, more intricate control mechanisms than simply this linear pathway, we analyzed  ...[more]

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