RapamycinFungusV1, Main, Exploration, bibRecord, 000883

Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2.

Identifieur interne : 000883 ( Main/Exploration ); précédent : 000882; suivant : 000884

Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2.

Auteurs : Manikandan Karuppasamy [France] ; Beata Kusmider [Suisse] ; Taiana M. Oliveira [France] ; Christl Gaubitz [Suisse] ; Manoel Prouteau [Suisse] ; Robbie Loewith [Suisse] ; Christiane Schaffitzel [France, Royaume-Uni]

Source :

Nature communications [ 2041-1723 ] ; 2017.

RBID : pubmed:29170376

Descripteurs français

English descriptors

KwdEn :
- Binding Sites (MeSH), Carrier Proteins (chemistry), Cryoelectron Microscopy (MeSH), Mechanistic Target of Rapamycin Complex 2 (chemistry), Mechanistic Target of Rapamycin Complex 2 (metabolism), Mechanistic Target of Rapamycin Complex 2 (ultrastructure), Models, Molecular (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Structure, Quaternary (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (ultrastructure), Transcription Factors (chemistry), Transcription Factors (metabolism), Transcription Factors (ultrastructure).
MESH :
- chemical , chemistry : Carrier Proteins, Mechanistic Target of Rapamycin Complex 2, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : Mechanistic Target of Rapamycin Complex 2, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , ultrastructure : Mechanistic Target of Rapamycin Complex 2, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Saccharomyces cerevisiae.
- Binding Sites, Cryoelectron Microscopy, Models, Molecular, Protein Interaction Domains and Motifs, Protein Structure, Quaternary.

Abstract

The target of rapamycin (TOR) kinase assembles into two distinct multiprotein complexes, conserved across eukaryote evolution. In contrast to TOR complex 1 (TORC1), TORC2 kinase activity is not inhibited by the macrolide rapamycin. Here, we present the structure of Saccharomyces cerevisiae TORC2 determined by electron cryo-microscopy. TORC2 contains six subunits assembling into a 1.4 MDa rhombohedron. Tor2 and Lst8 form the common core of both TOR complexes. Avo3/Rictor is unique to TORC2, but interacts with the same HEAT repeats of Tor2 that are engaged by Kog1/Raptor in mammalian TORC1, explaining the mutual exclusivity of these two proteins. Density, which we conclude is Avo3, occludes the FKBP12-rapamycin-binding site of Tor2's FRB domain rendering TORC2 rapamycin insensitive and recessing the kinase active site. Although mobile, Avo1/hSin1 further restricts access to the active site as its conserved-region-in-the-middle (CRIM) domain is positioned along an edge of the TORC2 active-site-cleft, consistent with a role for CRIM in substrate recruitment.

DOI: 10.1038/s41467-017-01862-0
PubMed: 29170376
PubMed Central: PMC5700991

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Carrier Proteins (chemistry)</term>
<term>Cryoelectron Microscopy (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (chemistry)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (ultrastructure)</term>
<term>Models, Molecular (MeSH)</term>
<term>Protein Interaction Domains and Motifs (MeSH)</term>
<term>Protein Structure, Quaternary (MeSH)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (ultrastructure)</term>
<term>Transcription Factors (chemistry)</term>
<term>Transcription Factors (metabolism)</term>
<term>Transcription Factors (ultrastructure)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine (composition chimique)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (ultrastructure)</term>
<term>Cryomicroscopie électronique (MeSH)</term>
<term>Facteurs de transcription (composition chimique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Facteurs de transcription (ultrastructure)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Motifs et domaines d'intéraction protéique (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (ultrastructure)</term>
<term>Protéines de transport (composition chimique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Structure quaternaire des protéines (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carrier Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de transport</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Cryoelectron Microscopy</term>
<term>Models, Molecular</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Structure, Quaternary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cryomicroscopie électronique</term>
<term>Modèles moléculaires</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Sites de fixation</term>
<term>Structure quaternaire des protéines</term>
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<front><div type="abstract" xml:lang="en">The target of rapamycin (TOR) kinase assembles into two distinct multiprotein complexes, conserved across eukaryote evolution. In contrast to TOR complex 1 (TORC1), TORC2 kinase activity is not inhibited by the macrolide rapamycin. Here, we present the structure of Saccharomyces cerevisiae TORC2 determined by electron cryo-microscopy. TORC2 contains six subunits assembling into a 1.4 MDa rhombohedron. Tor2 and Lst8 form the common core of both TOR complexes. Avo3/Rictor is unique to TORC2, but interacts with the same HEAT repeats of Tor2 that are engaged by Kog1/Raptor in mammalian TORC1, explaining the mutual exclusivity of these two proteins. Density, which we conclude is Avo3, occludes the FKBP12-rapamycin-binding site of Tor2's FRB domain rendering TORC2 rapamycin insensitive and recessing the kinase active site. Although mobile, Avo1/hSin1 further restricts access to the active site as its conserved-region-in-the-middle (CRIM) domain is positioned along an edge of the TORC2 active-site-cleft, consistent with a role for CRIM in substrate recruitment.</div>
</front>
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<DateCompleted><Year>2018</Year>
<Month>09</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>23</Day>
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<Issue>1</Issue>
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<Month>11</Month>
<Day>23</Day>
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<Title>Nature communications</Title>
<ISOAbbreviation>Nat Commun</ISOAbbreviation>
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<ArticleTitle>Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2.</ArticleTitle>
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<Abstract><AbstractText>The target of rapamycin (TOR) kinase assembles into two distinct multiprotein complexes, conserved across eukaryote evolution. In contrast to TOR complex 1 (TORC1), TORC2 kinase activity is not inhibited by the macrolide rapamycin. Here, we present the structure of Saccharomyces cerevisiae TORC2 determined by electron cryo-microscopy. TORC2 contains six subunits assembling into a 1.4 MDa rhombohedron. Tor2 and Lst8 form the common core of both TOR complexes. Avo3/Rictor is unique to TORC2, but interacts with the same HEAT repeats of Tor2 that are engaged by Kog1/Raptor in mammalian TORC1, explaining the mutual exclusivity of these two proteins. Density, which we conclude is Avo3, occludes the FKBP12-rapamycin-binding site of Tor2's FRB domain rendering TORC2 rapamycin insensitive and recessing the kinase active site. Although mobile, Avo1/hSin1 further restricts access to the active site as its conserved-region-in-the-middle (CRIM) domain is positioned along an edge of the TORC2 active-site-cleft, consistent with a role for CRIM in substrate recruitment.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Karuppasamy</LastName>
<ForeName>Manikandan</ForeName>
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<ForeName>Beata</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, Institute of Genetics and Genomics of Geneva (iGE3), University of Geneva, 30 Quai Ernest Ansermet, CH1211, Geneva, Switzerland.</Affiliation>
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	Serveur d'exploration sur la rapamycine et les champignons
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Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2.

Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2.

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