RapamycinFungusV1, Main, Exploration, bibRecord, 000846

Feedback Inhibition of the Rag GTPase GAP Complex Lst4-Lst7 Safeguards TORC1 from Hyperactivation by Amino Acid Signals.

Identifieur interne : 000846 ( Main/Exploration ); précédent : 000845; suivant : 000847

Feedback Inhibition of the Rag GTPase GAP Complex Lst4-Lst7 Safeguards TORC1 from Hyperactivation by Amino Acid Signals.

Auteurs : Marie-Pierre Péli-Gulli [Suisse] ; Serena Raucci [Suisse] ; Zehan Hu [Suisse] ; Jörn Dengjel [Suisse] ; Claudio De Virgilio [Suisse]

Source :

Cell reports [ 2211-1247 ] ; 2017.

RBID : pubmed:28700931

Descripteurs français

English descriptors

KwdEn :
- Immunoprecipitation (MeSH), Mass Spectrometry (MeSH), Mechanistic Target of Rapamycin Complex 1 (genetics), Mechanistic Target of Rapamycin Complex 1 (metabolism), Microscopy, Fluorescence (MeSH), Phosphorylation (MeSH), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (genetics), Signal Transduction (physiology), Transcription Factors (genetics), Transcription Factors (metabolism), Vesicular Transport Proteins (genetics), Vesicular Transport Proteins (metabolism).
MESH :
- chemical , genetics : Mechanistic Target of Rapamycin Complex 1, Saccharomyces cerevisiae Proteins, Transcription Factors, Vesicular Transport Proteins.
- chemical , metabolism : Mechanistic Target of Rapamycin Complex 1, Saccharomyces cerevisiae Proteins, Transcription Factors, Vesicular Transport Proteins.
- enzymology : Saccharomyces cerevisiae.
- genetics : Signal Transduction.
- metabolism : Saccharomyces cerevisiae.
- physiology : Signal Transduction.
- Immunoprecipitation, Mass Spectrometry, Microscopy, Fluorescence, Phosphorylation.

Abstract

Amino acids stimulate the eukaryotic target of rapamycin complex 1 (TORC1), and hence growth, through the Rag GTPases and their regulators. Among these, the yeast Lst4-Lst7 Rag GTPase GAP complex clusters, as we previously reported, at the vacuolar membrane upon amino acid starvation. In response to amino acid refeeding, it activates the Rag GTPase-TORC1 branch and is then dispersed from the vacuolar surface. Here, we show that the latter effect is driven by TORC1 itself, which directly phosphorylates several residues within the intra-DENN loop of Lst4 that, only in its non-phosphorylated state, tethers the Lst4-Lst7 complex to the vacuolar membrane. An Lst4 variant disrupting this feedback inhibition mechanism causes TORC1 hyperactivation and proliferation defects in cells grown on poor nitrogen sources. Thus, we identify Lst4 as a TORC1 target and key node of a homeostatic mechanism that adjusts TORC1 activity to the availability of amino acids.

DOI: 10.1016/j.celrep.2017.06.058
PubMed: 28700931

Affiliations:

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

to stream Main, to step Corpus: 000777
to stream Main, to step Curation: 000777

Le document en format XML

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<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Microscopy, Fluorescence (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
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<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Immunoprécipitation (MeSH)</term>
<term>Microscopie de fluorescence (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
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<term>Saccharomyces cerevisiae (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Amino acids stimulate the eukaryotic target of rapamycin complex 1 (TORC1), and hence growth, through the Rag GTPases and their regulators. Among these, the yeast Lst4-Lst7 Rag GTPase GAP complex clusters, as we previously reported, at the vacuolar membrane upon amino acid starvation. In response to amino acid refeeding, it activates the Rag GTPase-TORC1 branch and is then dispersed from the vacuolar surface. Here, we show that the latter effect is driven by TORC1 itself, which directly phosphorylates several residues within the intra-DENN loop of Lst4 that, only in its non-phosphorylated state, tethers the Lst4-Lst7 complex to the vacuolar membrane. An Lst4 variant disrupting this feedback inhibition mechanism causes TORC1 hyperactivation and proliferation defects in cells grown on poor nitrogen sources. Thus, we identify Lst4 as a TORC1 target and key node of a homeostatic mechanism that adjusts TORC1 activity to the availability of amino acids.</div>
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<Abstract><AbstractText>Amino acids stimulate the eukaryotic target of rapamycin complex 1 (TORC1), and hence growth, through the Rag GTPases and their regulators. Among these, the yeast Lst4-Lst7 Rag GTPase GAP complex clusters, as we previously reported, at the vacuolar membrane upon amino acid starvation. In response to amino acid refeeding, it activates the Rag GTPase-TORC1 branch and is then dispersed from the vacuolar surface. Here, we show that the latter effect is driven by TORC1 itself, which directly phosphorylates several residues within the intra-DENN loop of Lst4 that, only in its non-phosphorylated state, tethers the Lst4-Lst7 complex to the vacuolar membrane. An Lst4 variant disrupting this feedback inhibition mechanism causes TORC1 hyperactivation and proliferation defects in cells grown on poor nitrogen sources. Thus, we identify Lst4 as a TORC1 target and key node of a homeostatic mechanism that adjusts TORC1 activity to the availability of amino acids.</AbstractText>
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<settlement><li>Fribourg</li>
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<orgName><li>Université de Fribourg</li>
</orgName>
</list>
<tree><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Peli Gulli, Marie Pierre" sort="Peli Gulli, Marie Pierre" uniqKey="Peli Gulli M" first="Marie-Pierre" last="Péli-Gulli">Marie-Pierre Péli-Gulli</name>
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<name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name>
<name sortKey="Dengjel, Jorn" sort="Dengjel, Jorn" uniqKey="Dengjel J" first="Jörn" last="Dengjel">Jörn Dengjel</name>
<name sortKey="Hu, Zehan" sort="Hu, Zehan" uniqKey="Hu Z" first="Zehan" last="Hu">Zehan Hu</name>
<name sortKey="Raucci, Serena" sort="Raucci, Serena" uniqKey="Raucci S" first="Serena" last="Raucci">Serena Raucci</name>
</country>
</tree>
</affiliations>
</record>

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   |type=    RBID
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   |texte=   Feedback Inhibition of the Rag GTPase GAP Complex Lst4-Lst7 Safeguards TORC1 from Hyperactivation by Amino Acid Signals.
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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

Feedback Inhibition of the Rag GTPase GAP Complex Lst4-Lst7 Safeguards TORC1 from Hyperactivation by Amino Acid Signals.

Feedback Inhibition of the Rag GTPase GAP Complex Lst4-Lst7 Safeguards TORC1 from Hyperactivation by Amino Acid Signals.

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