The TOR‐dependent phosphoproteome and regulation of cellular protein synthesis |
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| Authors: | Tiffany Mak Andrew W Jones Paul Nurse |
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| Institution: | 1. Cell Cycle Laboratory, The Francis Crick Institute, London UK ; 2. Protein Analysis and Proteomics Platform, The Francis Crick Institute, London UK ; 3. Laboratory of Yeast Genetics and Cell Biology, Rockefeller University, New York NY, USA ;4.Present address: The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kgs. Lyngby Denmark |
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| Abstract: | Cell growth is orchestrated by a number of interlinking cellular processes. Components of the TOR pathway have been proposed as potential regulators of cell growth, but little is known about their immediate effects on protein synthesis in response to TOR‐dependent growth inhibition. Here, we present a resource providing an in‐depth characterisation of Schizosaccharomyces pombe phosphoproteome in relation to changes observed in global cellular protein synthesis upon TOR inhibition. We find that after TOR inhibition, the rate of protein synthesis is rapidly reduced and that notable phosphorylation changes are observed in proteins involved in a range of cellular processes. We show that this reduction in protein synthesis rates upon TOR inhibition is not dependent on S6K activity, but is partially dependent on the S. pombe homologue of eIF4G, Tif471. Our study demonstrates the impact of TOR‐dependent phospho‐regulation on the rate of protein synthesis and establishes a foundational resource for further investigation of additional TOR‐regulated targets both in fission yeast and other eukaryotes. |
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| Keywords: | phosphoproteomics protein synthesis TOR regulation |
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