RapamycinFungusV1, Main, Exploration, bibRecord, 001479

TORC1 controls degradation of the transcription factor Stp1, a key effector of the SPS amino-acid-sensing pathway in Saccharomyces cerevisiae.

Identifieur interne : 001479 ( Main/Exploration ); précédent : 001478; suivant : 001480

TORC1 controls degradation of the transcription factor Stp1, a key effector of the SPS amino-acid-sensing pathway in Saccharomyces cerevisiae.

Auteurs : Chun-Shik Shin [Corée du Sud] ; Sun Young Kim ; Won-Ki Huh

Source :

Journal of cell science [ 0021-9533 ] ; 2009.

RBID : pubmed:19494127

Descripteurs français

English descriptors

KwdEn :
- Amino Acids (metabolism), Antifungal Agents (pharmacology), Cell Nucleus (metabolism), Drug Resistance, Fungal (genetics), Genome, Fungal (drug effects), Nuclear Proteins (genetics), Nuclear Proteins (metabolism), Organisms, Genetically Modified (MeSH), Protein Kinases (genetics), Protein Kinases (metabolism), Protein Kinases (physiology), Protein Processing, Post-Translational (genetics), Quorum Sensing (genetics), Quorum Sensing (physiology), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (physiology), Signal Transduction (genetics), Signal Transduction (physiology), Sirolimus (pharmacology), TOR Serine-Threonine Kinases (MeSH), Transcription Factors (genetics), Transcription Factors (metabolism).
MESH :
- chemical , genetics : Nuclear Proteins, Protein Kinases, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : Amino Acids, Nuclear Proteins, Protein Kinases, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents, Sirolimus.
- drug effects : Genome, Fungal.
- genetics : Drug Resistance, Fungal, Protein Processing, Post-Translational, Quorum Sensing, Saccharomyces cerevisiae, Signal Transduction.
- metabolism : Cell Nucleus, Saccharomyces cerevisiae.
- chemical , physiology : Protein Kinases, Quorum Sensing, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction.
- Organisms, Genetically Modified, TOR Serine-Threonine Kinases.

Abstract

The target of rapamycin (TOR) signaling pathway plays crucial roles in the regulation of eukaryotic cell growth. In Saccharomyces cerevisiae, nitrogen sources in the extracellular environment activate the TOR signaling pathway. However, the precise mechanisms underlying the regulation of TOR activity in response to extracellular nitrogen sources are poorly understood. Here, we report that degradation of Stp1, a transcription factor for amino acid uptake and a key effector of the SPS amino-acid-sensing pathway, is controlled by TOR activity in S. cerevisiae. Using a genome-wide protein localization study, we found that Stp1 disappeared from the nucleus upon inactivation of TOR complex 1 (TORC1) by rapamycin, suggesting the involvement of Stp1 in the TOR signaling pathway. Supporting this notion, a knockout mutant for the STP1 gene was found to be hypersensitive to rapamycin, and overexpression of STP1 conferred resistance to rapamycin. Interestingly, we found that the rapamycin-induced disappearance of Stp1 from the nucleus resulted from Stp1 degradation, which was dependent on the activity of a protein phosphatase 2A (PP2A)-like phosphatase, Sit4, which is a well-known downstream effector of TORC1. Taken together, our findings highlight an intimate connection between the amino-acid-sensing pathway and the rapamycin-sensitive TOR signaling pathway.

DOI: 10.1242/jcs.047191
PubMed: 19494127

Affiliations:

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

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Le document en format XML

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<term>Antifungal Agents (pharmacology)</term>
<term>Cell Nucleus (metabolism)</term>
<term>Drug Resistance, Fungal (genetics)</term>
<term>Genome, Fungal (drug effects)</term>
<term>Nuclear Proteins (genetics)</term>
<term>Nuclear Proteins (metabolism)</term>
<term>Organisms, Genetically Modified (MeSH)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Protein Kinases (physiology)</term>
<term>Protein Processing, Post-Translational (genetics)</term>
<term>Quorum Sensing (genetics)</term>
<term>Quorum Sensing (physiology)</term>
<term>RNA-Binding Proteins (genetics)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae (physiology)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (physiology)</term>
<term>Signal Transduction (genetics)</term>
<term>Signal Transduction (physiology)</term>
<term>Sirolimus (pharmacology)</term>
<term>TOR Serine-Threonine Kinases (MeSH)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term>
<term>Antifongiques (pharmacologie)</term>
<term>Détection du quorum (génétique)</term>
<term>Détection du quorum (physiologie)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Génome fongique (effets des médicaments et des substances chimiques)</term>
<term>Maturation post-traductionnelle des protéines (génétique)</term>
<term>Noyau de la cellule (métabolisme)</term>
<term>Organismes génétiquement modifiés (MeSH)</term>
<term>Protein kinases (génétique)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protein kinases (physiologie)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (physiologie)</term>
<term>Protéines de liaison à l'ARN (génétique)</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
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<term>Protéines nucléaires (métabolisme)</term>
<term>Résistance des champignons aux médicaments (génétique)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (physiologie)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Sérine-thréonine kinases TOR (MeSH)</term>
<term>Transduction du signal (génétique)</term>
<term>Transduction du signal (physiologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nuclear Proteins</term>
<term>Protein Kinases</term>
<term>RNA-Binding Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term>
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<term>Protein Kinases</term>
<term>RNA-Binding Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
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<term>Sirolimus</term>
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<term>Protein Processing, Post-Translational</term>
<term>Quorum Sensing</term>
<term>Saccharomyces cerevisiae</term>
<term>Signal Transduction</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Détection du quorum</term>
<term>Facteurs de transcription</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines nucléaires</term>
<term>Résistance des champignons aux médicaments</term>
<term>Saccharomyces cerevisiae</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term>
<term>Facteurs de transcription</term>
<term>Noyau de la cellule</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines nucléaires</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term>
<term>Sirolimus</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Détection du quorum</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Protein Kinases</term>
<term>Quorum Sensing</term>
<term>Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Organisms, Genetically Modified</term>
<term>TOR Serine-Threonine Kinases</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Organismes génétiquement modifiés</term>
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<front><div type="abstract" xml:lang="en">The target of rapamycin (TOR) signaling pathway plays crucial roles in the regulation of eukaryotic cell growth. In Saccharomyces cerevisiae, nitrogen sources in the extracellular environment activate the TOR signaling pathway. However, the precise mechanisms underlying the regulation of TOR activity in response to extracellular nitrogen sources are poorly understood. Here, we report that degradation of Stp1, a transcription factor for amino acid uptake and a key effector of the SPS amino-acid-sensing pathway, is controlled by TOR activity in S. cerevisiae. Using a genome-wide protein localization study, we found that Stp1 disappeared from the nucleus upon inactivation of TOR complex 1 (TORC1) by rapamycin, suggesting the involvement of Stp1 in the TOR signaling pathway. Supporting this notion, a knockout mutant for the STP1 gene was found to be hypersensitive to rapamycin, and overexpression of STP1 conferred resistance to rapamycin. Interestingly, we found that the rapamycin-induced disappearance of Stp1 from the nucleus resulted from Stp1 degradation, which was dependent on the activity of a protein phosphatase 2A (PP2A)-like phosphatase, Sit4, which is a well-known downstream effector of TORC1. Taken together, our findings highlight an intimate connection between the amino-acid-sensing pathway and the rapamycin-sensitive TOR signaling pathway.</div>
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<tree><noCountry><name sortKey="Huh, Won Ki" sort="Huh, Won Ki" uniqKey="Huh W" first="Won-Ki" last="Huh">Won-Ki Huh</name>
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<country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Shin, Chun Shik" sort="Shin, Chun Shik" uniqKey="Shin C" first="Chun-Shik" last="Shin">Chun-Shik Shin</name>
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   |area=    RapamycinFungusV1
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   |type=    RBID
   |clé=     pubmed:19494127
   |texte=   TORC1 controls degradation of the transcription factor Stp1, a key effector of the SPS amino-acid-sensing pathway in Saccharomyces cerevisiae.
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

TORC1 controls degradation of the transcription factor Stp1, a key effector of the SPS amino-acid-sensing pathway in Saccharomyces cerevisiae.

TORC1 controls degradation of the transcription factor Stp1, a key effector of the SPS amino-acid-sensing pathway in Saccharomyces cerevisiae.

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