RapamycinFungusV1, Main, Exploration, bibRecord, 001536

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis.

Identifieur interne : 001536 ( Main/Exploration ); précédent : 001535; suivant : 001537

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis.

Auteurs : Alexandre Huber [Suisse] ; Bernd Bodenmiller ; Aino Uotila ; Michael Stahl ; Stefanie Wanka ; Bertran Gerrits ; Ruedi Aebersold ; Robbie Loewith

Source :

Genes & development [ 1549-5477 ] ; 2009.

RBID : pubmed:19684113

Descripteurs français

KwdFr :
- Antifongiques (pharmacologie), Biosynthèse des protéines (physiologie), Cycloheximide (pharmacologie), Facteurs de transcription (métabolisme), Inhibiteurs de la synthèse protéique (pharmacologie), Liaison aux protéines (MeSH), Phosphorylation (effets des médicaments et des substances chimiques), Protein-Serine-Threonine Kinases (métabolisme), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéome (effets des médicaments et des substances chimiques), RNA polymerase I (métabolisme), RNA polymerase III (métabolisme), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (physiologie), Sirolimus (pharmacologie), Transduction du signal (MeSH), Transport des protéines (MeSH).
MESH :
- effets des médicaments et des substances chimiques : Phosphorylation, Protéome.
- enzymologie : Saccharomyces cerevisiae.
- métabolisme : Facteurs de transcription, Protein-Serine-Threonine Kinases, Protéines adaptatrices de la transduction du signal, Protéines de Saccharomyces cerevisiae, RNA polymerase I, RNA polymerase III, Saccharomyces cerevisiae.
- pharmacologie : Antifongiques, Cycloheximide, Inhibiteurs de la synthèse protéique, Sirolimus.
- physiologie : Biosynthèse des protéines, Saccharomyces cerevisiae.
- Liaison aux protéines, Transduction du signal, Transport des protéines.

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (metabolism), Antifungal Agents (pharmacology), Cycloheximide (pharmacology), Phosphorylation (drug effects), Protein Binding (MeSH), Protein Biosynthesis (physiology), Protein Synthesis Inhibitors (pharmacology), Protein Transport (MeSH), Protein-Serine-Threonine Kinases (metabolism), Proteome (drug effects), RNA Polymerase I (metabolism), RNA Polymerase III (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sirolimus (pharmacology), Transcription Factors (metabolism).
MESH :
- chemical , drug effects : Proteome.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Protein-Serine-Threonine Kinases, RNA Polymerase I, RNA Polymerase III, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents, Cycloheximide, Protein Synthesis Inhibitors, Sirolimus.
- drug effects : Phosphorylation.
- enzymology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- physiology : Protein Biosynthesis, Saccharomyces cerevisiae.
- Protein Binding, Protein Transport, Signal Transduction.

Abstract

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.

DOI: 10.1101/gad.532109
PubMed: 19684113
PubMed Central: PMC2725941

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001489
to stream Main, to step Curation: 001489

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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	Serveur d'exploration sur la rapamycine et les champignons
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Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis.

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis.

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