RapamycinFungusV1, Main, Exploration, bibRecord, 000973

Tor forms a dimer through an N-terminal helical solenoid with a complex topology.

Identifieur interne : 000973 ( Main/Exploration ); précédent : 000972; suivant : 000974

Tor forms a dimer through an N-terminal helical solenoid with a complex topology.

Auteurs : Domagoj Bareti [Royaume-Uni] ; Alex Berndt [Royaume-Uni] ; Yohei Ohashi [Royaume-Uni] ; Christopher M. Johnson [Royaume-Uni] ; Roger L. Williams [Royaume-Uni]

Source :

Nature communications [ 2041-1723 ] ; 2016.

RBID : pubmed:27072897

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Catalytic Domain (MeSH), Cryoelectron Microscopy (MeSH), Humans (MeSH), Kluyveromyces (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mechanistic Target of Rapamycin Complex 2 (MeSH), Mice (MeSH), Models, Molecular (MeSH), Multiprotein Complexes (chemistry), Multiprotein Complexes (metabolism), Multiprotein Complexes (ultrastructure), Protein Binding (MeSH), Protein Multimerization (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), TOR Serine-Threonine Kinases (chemistry), TOR Serine-Threonine Kinases (metabolism), TOR Serine-Threonine Kinases (ultrastructure).
MESH :
- chemical , chemistry : Multiprotein Complexes, TOR Serine-Threonine Kinases.
- chemical , metabolism : Multiprotein Complexes, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- chemical , ultrastructure : Multiprotein Complexes, TOR Serine-Threonine Kinases.
- chemical : Mechanistic Target of Rapamycin Complex 1, Mechanistic Target of Rapamycin Complex 2.
- metabolism : Kluyveromyces, Saccharomyces cerevisiae.
- Animals, Catalytic Domain, Cryoelectron Microscopy, Humans, Mice, Models, Molecular, Protein Binding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary.

Abstract

The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of Tor form a HEAT repeat-containing α-solenoid with four distinct segments: a highly curved 800-residue N-terminal 'spiral', followed by a 400-residue low-curvature 'bridge' and an extended 'railing' running along the bridge leading to the 'cap' that links to FAT region. This complex topology was verified by domain insertions and offers a new interpretation of the mTORC1 structure. The spiral of one TOR interacts with the bridge of another, which together form a joint platform for the Regulatory Associated Protein of TOR (RAPTOR) regulatory subunit.

DOI: 10.1038/ncomms11016
PubMed: 27072897
PubMed Central: PMC4833857

Affiliations:

Royaume-Uni

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

to stream Main, to step Corpus: 000A64
to stream Main, to step Curation: 000A64

Le document en format XML

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<term>Catalytic Domain (MeSH)</term>
<term>Cryoelectron Microscopy (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Kluyveromyces (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Multiprotein Complexes (chemistry)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Multiprotein Complexes (ultrastructure)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
<term>Protein Structure, Secondary (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>TOR Serine-Threonine Kinases (chemistry)</term>
<term>TOR Serine-Threonine Kinases (metabolism)</term>
<term>TOR Serine-Threonine Kinases (ultrastructure)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (composition chimique)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Complexes multiprotéiques (ultrastructure)</term>
<term>Cryomicroscopie électronique (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Kluyveromyces (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Multimérisation de protéines (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Souris (MeSH)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Sérine-thréonine kinases TOR (composition chimique)</term>
<term>Sérine-thréonine kinases TOR (métabolisme)</term>
<term>Sérine-thréonine kinases TOR (ultrastructure)</term>
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<term>TOR Serine-Threonine Kinases</term>
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<term>Saccharomyces cerevisiae Proteins</term>
<term>TOR Serine-Threonine Kinases</term>
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<term>TOR Serine-Threonine Kinases</term>
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<term>Mechanistic Target of Rapamycin Complex 2</term>
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<term>Sérine-thréonine kinases TOR</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Kluyveromyces</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Kluyveromyces</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
<term>Sérine-thréonine kinases TOR</term>
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<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Complexes multiprotéiques</term>
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<term>Catalytic Domain</term>
<term>Cryoelectron Microscopy</term>
<term>Humans</term>
<term>Mice</term>
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Complexe-2 cible mécanistique de la rapamycine</term>
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<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
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<front><div type="abstract" xml:lang="en">The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of Tor form a HEAT repeat-containing α-solenoid with four distinct segments: a highly curved 800-residue N-terminal 'spiral', followed by a 400-residue low-curvature 'bridge' and an extended 'railing' running along the bridge leading to the 'cap' that links to FAT region. This complex topology was verified by domain insertions and offers a new interpretation of the mTORC1 structure. The spiral of one TOR interacts with the bridge of another, which together form a joint platform for the Regulatory Associated Protein of TOR (RAPTOR) regulatory subunit. </div>
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<Abstract><AbstractText>The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of Tor form a HEAT repeat-containing α-solenoid with four distinct segments: a highly curved 800-residue N-terminal 'spiral', followed by a 400-residue low-curvature 'bridge' and an extended 'railing' running along the bridge leading to the 'cap' that links to FAT region. This complex topology was verified by domain insertions and offers a new interpretation of the mTORC1 structure. The spiral of one TOR interacts with the bridge of another, which together form a joint platform for the Regulatory Associated Protein of TOR (RAPTOR) regulatory subunit. </AbstractText>
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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

Tor forms a dimer through an N-terminal helical solenoid with a complex topology.

Tor forms a dimer through an N-terminal helical solenoid with a complex topology.

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