RapamycinFungusV1, Main, Exploration, bibRecord, 000D23

Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling.

Identifieur interne : 000D23 ( Main/Exploration ); précédent : 000D22; suivant : 000D24

Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling.

Auteurs : Katie Powis [Suisse] ; Tianlong Zhang [République populaire de Chine] ; Nicolas Panchaud [Suisse] ; Rong Wang [République populaire de Chine] ; Claudio De Virgilio [Suisse] ; Jianping Ding [République populaire de Chine]

Source :

Cell research [ 1748-7838 ] ; 2015.

RBID : pubmed:26206314

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Crystallography, X-Ray (MeSH), Immunoprecipitation (MeSH), Molecular Sequence Data (MeSH), Monomeric GTP-Binding Proteins (metabolism), Phosphorylation (MeSH), Protein Structure, Quaternary (MeSH), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Signal Transduction (MeSH), Transcription Factors (metabolism).
MESH :
- chemical , chemistry : Saccharomyces cerevisiae Proteins.
- chemical , genetics : Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Monomeric GTP-Binding Proteins, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Saccharomyces cerevisiae.
- Amino Acid Sequence, Crystallography, X-Ray, Immunoprecipitation, Molecular Sequence Data, Phosphorylation, Protein Structure, Quaternary, Sequence Alignment, Sequence Homology, Amino Acid, Signal Transduction.

Abstract

The target of rapamycin complex 1 (TORC1) integrates various hormonal and nutrient signals to regulate cell growth, proliferation, and differentiation. Amino acid-dependent activation of TORC1 is mediated via the yeast EGO complex (EGOC) consisting of Gtr1, Gtr2, Ego1, and Ego3. Here, we identify the previously uncharacterized Ycr075w-a/Ego2 protein as an additional EGOC component that is required for the integrity and localization of the heterodimeric Gtr1-Gtr2 GTPases, equivalent to mammalian Rag GTPases. We also report the crystal structure of the Ego1-Ego2-Ego3 ternary complex (EGO-TC) at 2.4 Å resolution, in which Ego2 and Ego3 form a heterodimer flanked along one side by Ego1. Structural data also reveal the structural conservation of protein components between the yeast EGO-TC and the human Ragulator, which acts as a GEF for Rag GTPases. Interestingly, however, artificial tethering of Gtr1-Gtr2 to the vacuolar membrane is sufficient to activate TORC1 in response to amino acids even in the absence of the EGO-TC. Our structural and functional data therefore support a model in which the EGO-TC acts as a scaffold for Rag GTPases in TORC1 signaling.

DOI: 10.1038/cr.2015.86
PubMed: 26206314
PubMed Central: PMC4559812

Affiliations:

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

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Le document en format XML

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<term>Crystallography, X-Ray (MeSH)</term>
<term>Immunoprecipitation (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Monomeric GTP-Binding Proteins (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Structure, Quaternary (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
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<term>Facteurs de transcription (métabolisme)</term>
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<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines G monomériques (métabolisme)</term>
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<term>Protéines de Saccharomyces cerevisiae</term>
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<term>Immunoprecipitation</term>
<term>Molecular Sequence Data</term>
<term>Phosphorylation</term>
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<term>Signal Transduction</term>
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<front><div type="abstract" xml:lang="en">The target of rapamycin complex 1 (TORC1) integrates various hormonal and nutrient signals to regulate cell growth, proliferation, and differentiation. Amino acid-dependent activation of TORC1 is mediated via the yeast EGO complex (EGOC) consisting of Gtr1, Gtr2, Ego1, and Ego3. Here, we identify the previously uncharacterized Ycr075w-a/Ego2 protein as an additional EGOC component that is required for the integrity and localization of the heterodimeric Gtr1-Gtr2 GTPases, equivalent to mammalian Rag GTPases. We also report the crystal structure of the Ego1-Ego2-Ego3 ternary complex (EGO-TC) at 2.4 Å resolution, in which Ego2 and Ego3 form a heterodimer flanked along one side by Ego1. Structural data also reveal the structural conservation of protein components between the yeast EGO-TC and the human Ragulator, which acts as a GEF for Rag GTPases. Interestingly, however, artificial tethering of Gtr1-Gtr2 to the vacuolar membrane is sufficient to activate TORC1 in response to amino acids even in the absence of the EGO-TC. Our structural and functional data therefore support a model in which the EGO-TC acts as a scaffold for Rag GTPases in TORC1 signaling. </div>
</front>
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<Abstract><AbstractText>The target of rapamycin complex 1 (TORC1) integrates various hormonal and nutrient signals to regulate cell growth, proliferation, and differentiation. Amino acid-dependent activation of TORC1 is mediated via the yeast EGO complex (EGOC) consisting of Gtr1, Gtr2, Ego1, and Ego3. Here, we identify the previously uncharacterized Ycr075w-a/Ego2 protein as an additional EGOC component that is required for the integrity and localization of the heterodimeric Gtr1-Gtr2 GTPases, equivalent to mammalian Rag GTPases. We also report the crystal structure of the Ego1-Ego2-Ego3 ternary complex (EGO-TC) at 2.4 Å resolution, in which Ego2 and Ego3 form a heterodimer flanked along one side by Ego1. Structural data also reveal the structural conservation of protein components between the yeast EGO-TC and the human Ragulator, which acts as a GEF for Rag GTPases. Interestingly, however, artificial tethering of Gtr1-Gtr2 to the vacuolar membrane is sufficient to activate TORC1 in response to amino acids even in the absence of the EGO-TC. Our structural and functional data therefore support a model in which the EGO-TC acts as a scaffold for Rag GTPases in TORC1 signaling. </AbstractText>
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Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling.

Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling.

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