The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates.
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ABSTRACT: Regulation of cell growth requires extensive coordination of several processes including transcription, ribosome biogenesis, translation, nutrient metabolism, and autophagy. In yeast, the protein kinases Target of Rapamycin (TOR) and protein kinase A (PKA) regulate these processes and are thereby the main activators of cell growth in response to nutrients. How TOR, PKA, and their corresponding signaling pathways are coordinated to control the same cellular processes is not understood. Quantitative analysis of the rapamycin-sensitive phosphoproteome combined with targeted analysis of PKA substrates suggests that TOR complex 1 (TORC1) activates PKA but only toward a subset of substrates. Furthermore, we show that TORC1 signaling impinges on BCY1, the negative regulatory subunit of PKA. Inhib
SUBMITTER: Soulard A
PROVIDER: S-EPMC2947482 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
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