Journal
GENES & DEVELOPMENT
Volume 23, Issue 16, Pages 1929-1943Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.532109
Keywords
Maf1; Sch9; TOR; phosphoproteomics; rapamycin; ribosome biogenesis
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Funding
- ETH Zurich
- Swiss National Science Foundation [31000-10767, PP00P3-110770/3100A0-108114]
- National Heart, Lung, and Blood Institute, National Institutes of Health [N01-HV-28179]
- SystemsX. ch,
- Swiss initiative for systems biology
- University Research Priority Program Systems Biology
- F. Hoffmann-La Roche Ltd. ( Basel, Switzerland)
- Boehringer Ingelheim Fonds
- Novartis Foundation for Biology and Medicine
- Roche Research Foundation
- canton of Geneve
- Leenaards Foundation
- European Research Council [ERC-2007-StG206173-TOR]
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The target of rapamycin complex 1 (TORC1) is an essential multiprotein complex conserved from yeast to humans. Under favorable growth conditions, and in the absence of the macrolide rapamycin, TORC1 is active, and influences virtually all aspects of cell growth. Although two direct effectors of yeast TORC1 have been reported (Tap42, a regulator of PP2A phosphatases and Sch9, an AGC family kinase), the signaling pathways that couple TORC1 to its distal effectors were not well understood. To elucidate these pathways we developed and employed a quantitative, label-free mass spectrometry approach. Analyses of the rapamycin-sensitive phosphoproteomes in various genetic backgrounds revealed both documented and novel TORC1 effectors and allowed us to partition phosphorylation events between Tap42 and Sch9. Follow-up detailed characterization shows that Sch9 regulates RNA polymerases I and III, the latter via Maf1, in addition to translation initiation and the expression of ribosomal protein and ribosome biogenesis genes. This demonstrates that Sch9 is a master regulator of protein synthesis.
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