RapamycinFungusV1, Main, Exploration, bibRecord, 001137

Psk1, an AGC kinase family member in fission yeast, is directly phosphorylated and controlled by TORC1 and functions as S6 kinase.

Identifieur interne : 001137 ( Main/Exploration ); précédent : 001136; suivant : 001138

Psk1, an AGC kinase family member in fission yeast, is directly phosphorylated and controlled by TORC1 and functions as S6 kinase.

Auteurs : Akio Nakashima [États-Unis] ; Yoko Otsubo ; Akira Yamashita ; Tatsuhiro Sato ; Masayuki Yamamoto ; Fuyuhiko Tamanoi

Source :

Journal of cell science [ 1477-9137 ] ; 2012.

RBID : pubmed:22976295

Descripteurs français

English descriptors

KwdEn :
- Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Phosphorylation (genetics), Phosphorylation (physiology), Protein-Serine-Threonine Kinases (metabolism), Ribosomal Protein S6 Kinases (genetics), Ribosomal Protein S6 Kinases (metabolism), Schizosaccharomyces (enzymology), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Signal Transduction (genetics), Signal Transduction (physiology), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism).
MESH :
- chemical , genetics : Multiprotein Complexes, Ribosomal Protein S6 Kinases, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- chemical , metabolism : Multiprotein Complexes, Protein-Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, Schizosaccharomyces pombe Proteins, TOR Serine-Threonine Kinases.
- chemical : Mechanistic Target of Rapamycin Complex 1.
- enzymology : Schizosaccharomyces.
- genetics : Phosphorylation, Schizosaccharomyces, Signal Transduction.
- metabolism : Schizosaccharomyces.
- physiology : Phosphorylation, Signal Transduction.

Abstract

Target of rapamycin (TOR), an evolutionarily conserved serine/threonine protein kinase, plays pivotal roles in several important cellular processes in eukaryotes. In the fission yeast Schizosaccharomyces pombe, TOR complex 1 (TORC1), which includes Tor2 as a catalytic subunit, manages the switch between cell proliferation and differentiation by sensing nutrient availability. However, little is known about the direct target of TORC1 that plays key roles in nutrient-dependent TORC1 signaling in fission yeast. Here we report that in fission yeast, three AGC kinase family members, named Psk1, Sck1 and Sck2, which exhibit high homology with human S6K1, are phosphorylated under nutrient-rich conditions and are dephosphorylated by starvation conditions. Among these, Psk1 is necessary for phosphorylation of ribosomal protein S6. Furthermore, Psk1 phosphorylation is regulated by TORC1 in nutrient-dependent and rapamycin-sensitive manners in vivo. Three conserved regulatory motifs (the activation loop, the hydrophobic and the turn motifs) in Psk1 are phosphorylated and these modifications are required for Psk1 activity. In particular, phosphorylation of the hydrophobic motif is catalyzed by TORC1 in vivo and in vitro. Ksg1, a homolog of PDK1, is also important for Psk1 phosphorylation in the activation loop and for its activity. The TORC1 components Pop3, Toc1 and Tco89, are dispensable for Psk1 regulation, but disruption of pop3(+) causes an increase in the sensitivity of TORC1 to rapamycin. Taken together, these results provide convincing evidence that TORC1/Psk1/Rps6 constitutes a nutrient-dependent signaling pathway in fission yeast.

DOI: 10.1242/jcs.111146
PubMed: 22976295
PubMed Central: PMC3575713

Affiliations:

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

to stream Main, to step Corpus: 001108
to stream Main, to step Curation: 001108

Le document en format XML

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<term>Multiprotein Complexes (metabolism)</term>
<term>Phosphorylation (genetics)</term>
<term>Phosphorylation (physiology)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
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<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
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<term>TOR Serine-Threonine Kinases (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (génétique)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Phosphorylation (génétique)</term>
<term>Phosphorylation (physiologie)</term>
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<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
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<term>Schizosaccharomyces (génétique)</term>
<term>Schizosaccharomyces (métabolisme)</term>
<term>Sérine-thréonine kinases TOR (génétique)</term>
<term>Sérine-thréonine kinases TOR (métabolisme)</term>
<term>Transduction du signal (génétique)</term>
<term>Transduction du signal (physiologie)</term>
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<term>TOR Serine-Threonine Kinases</term>
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<term>Ribosomal Protein S6 Kinases</term>
<term>Schizosaccharomyces pombe Proteins</term>
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<term>Protéines de Schizosaccharomyces pombe</term>
<term>Ribosomal Protein S6 Kinases</term>
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<front><div type="abstract" xml:lang="en">Target of rapamycin (TOR), an evolutionarily conserved serine/threonine protein kinase, plays pivotal roles in several important cellular processes in eukaryotes. In the fission yeast Schizosaccharomyces pombe, TOR complex 1 (TORC1), which includes Tor2 as a catalytic subunit, manages the switch between cell proliferation and differentiation by sensing nutrient availability. However, little is known about the direct target of TORC1 that plays key roles in nutrient-dependent TORC1 signaling in fission yeast. Here we report that in fission yeast, three AGC kinase family members, named Psk1, Sck1 and Sck2, which exhibit high homology with human S6K1, are phosphorylated under nutrient-rich conditions and are dephosphorylated by starvation conditions. Among these, Psk1 is necessary for phosphorylation of ribosomal protein S6. Furthermore, Psk1 phosphorylation is regulated by TORC1 in nutrient-dependent and rapamycin-sensitive manners in vivo. Three conserved regulatory motifs (the activation loop, the hydrophobic and the turn motifs) in Psk1 are phosphorylated and these modifications are required for Psk1 activity. In particular, phosphorylation of the hydrophobic motif is catalyzed by TORC1 in vivo and in vitro. Ksg1, a homolog of PDK1, is also important for Psk1 phosphorylation in the activation loop and for its activity. The TORC1 components Pop3, Toc1 and Tco89, are dispensable for Psk1 regulation, but disruption of pop3(+) causes an increase in the sensitivity of TORC1 to rapamycin. Taken together, these results provide convincing evidence that TORC1/Psk1/Rps6 constitutes a nutrient-dependent signaling pathway in fission yeast.</div>
</front>
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<Abstract><AbstractText>Target of rapamycin (TOR), an evolutionarily conserved serine/threonine protein kinase, plays pivotal roles in several important cellular processes in eukaryotes. In the fission yeast Schizosaccharomyces pombe, TOR complex 1 (TORC1), which includes Tor2 as a catalytic subunit, manages the switch between cell proliferation and differentiation by sensing nutrient availability. However, little is known about the direct target of TORC1 that plays key roles in nutrient-dependent TORC1 signaling in fission yeast. Here we report that in fission yeast, three AGC kinase family members, named Psk1, Sck1 and Sck2, which exhibit high homology with human S6K1, are phosphorylated under nutrient-rich conditions and are dephosphorylated by starvation conditions. Among these, Psk1 is necessary for phosphorylation of ribosomal protein S6. Furthermore, Psk1 phosphorylation is regulated by TORC1 in nutrient-dependent and rapamycin-sensitive manners in vivo. Three conserved regulatory motifs (the activation loop, the hydrophobic and the turn motifs) in Psk1 are phosphorylated and these modifications are required for Psk1 activity. In particular, phosphorylation of the hydrophobic motif is catalyzed by TORC1 in vivo and in vitro. Ksg1, a homolog of PDK1, is also important for Psk1 phosphorylation in the activation loop and for its activity. The TORC1 components Pop3, Toc1 and Tco89, are dispensable for Psk1 regulation, but disruption of pop3(+) causes an increase in the sensitivity of TORC1 to rapamycin. Taken together, these results provide convincing evidence that TORC1/Psk1/Rps6 constitutes a nutrient-dependent signaling pathway in fission yeast.</AbstractText>
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Serveur d'exploration sur la rapamycine et les champignons

Psk1, an AGC kinase family member in fission yeast, is directly phosphorylated and controlled by TORC1 and functions as S6 kinase.

Psk1, an AGC kinase family member in fission yeast, is directly phosphorylated and controlled by TORC1 and functions as S6 kinase.

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