Journal
EMBO JOURNAL
Volume 40, Issue 16, Pages -Publisher
WILEY
DOI: 10.15252/embj.2021107911
Keywords
phosphoproteomics; protein synthesis; TOR regulation
Categories
Funding
- Francis Crick Institute from Cancer Research UK [FC01121]
- UK Medical Research Council [FC01121]
- Wellcome Trust [FC01121, 214183, 093917]
- Lord Leonard and Lady Estelle Wolfson Foundation
- Woosnam Foundation
- Breast Cancer Research Foundation [BCRF-20-117]
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The study delves into how the TOR pathway regulates cellular protein synthesis, showing that protein synthesis rate decreases significantly after TOR inhibition, impacting various cellular processes.
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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