RapamycinFungusV1, Main, Exploration, bibRecord, 000509

Redesigning TOR Kinase to Explore the Structural Basis for TORC1 and TORC2 Assembly.

Identifieur interne : 000509 ( Main/Exploration ); précédent : 000508; suivant : 000510

Redesigning TOR Kinase to Explore the Structural Basis for TORC1 and TORC2 Assembly.

Auteurs : Andrew Hill [États-Unis] ; Brad Niles [États-Unis] ; Andrew Cuyegkeng [États-Unis] ; Ted Powers [États-Unis]

Source :

Biomolecules [ 2218-273X ] ; 2018.

RBID : pubmed:29865216

Descripteurs français

KwdFr :
- Complexe-1 cible mécanistique de la rapamycine (métabolisme), Complexe-2 cible mécanistique de la rapamycine (métabolisme), Domaines protéiques (MeSH), Liaison aux protéines (MeSH), Multimérisation de protéines (MeSH), Phosphatidylinositol 3-kinases (composition chimique), Phosphatidylinositol 3-kinases (génétique), Phosphatidylinositol 3-kinases (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du cycle cellulaire (composition chimique), Protéines du cycle cellulaire (génétique), Protéines du cycle cellulaire (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme).
MESH :
- composition chimique : Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire.
- génétique : Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Saccharomyces cerevisiae.
- métabolisme : Complexe-1 cible mécanistique de la rapamycine, Complexe-2 cible mécanistique de la rapamycine, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Saccharomyces cerevisiae.
- Domaines protéiques, Liaison aux protéines, Multimérisation de protéines.

English descriptors

KwdEn :
- Cell Cycle Proteins (chemistry), Cell Cycle Proteins (genetics), Cell Cycle Proteins (metabolism), Mechanistic Target of Rapamycin Complex 1 (metabolism), Mechanistic Target of Rapamycin Complex 2 (metabolism), Phosphatidylinositol 3-Kinases (chemistry), Phosphatidylinositol 3-Kinases (genetics), Phosphatidylinositol 3-Kinases (metabolism), Protein Binding (MeSH), Protein Domains (MeSH), Protein Multimerization (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
MESH :
- chemical , chemistry : Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Cell Cycle Proteins, Mechanistic Target of Rapamycin Complex 1, Mechanistic Target of Rapamycin Complex 2, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Protein Binding, Protein Domains, Protein Multimerization.

Abstract

TOR is a serine/threonine protein kinase that assembles into distinct TOR Complexes 1 and 2 (TORC1 or TORC2) to regulate cell growth. In mammalian cells, a single mTOR incorporates stably into mTORC1 and mTORC2. By contrast, in Saccharomyces cerevisiae, two highly similar Tor1 and Tor2 proteins exist, where Tor1 assembles exclusively into TORC1 and Tor2 assembles preferentially into TORC2. To gain insight into TOR complex assembly, we used this bifurcation in yeast to identify structural elements within Tor1 and Tor2 that govern their complex specificity. We have identified a concise region of ~500 amino acids within the N-terminus of Tor2, which we term the Major Assembly Specificity (MAS) domain, that is sufficient to confer significant TORC2 activity when placed into an otherwise Tor1 protein. Consistently, introduction of the corresponding MAS domain from Tor1 into an otherwise Tor2 is sufficient to confer stable association with TORC1-specific components. Remarkably, much like mTOR, this latter chimera also retains stable interactions with TORC2 components, indicating that determinants throughout Tor1/Tor2 contribute to complex specificity. Our findings are in excellent agreement with recent ultrastructural studies of TORC1 and TORC2, where the MAS domain is involved in quaternary interactions important for complex formation and/or stability.

DOI: 10.3390/biom8020036
PubMed: 29865216
PubMed Central: PMC6023025

Affiliations:

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

to stream Main, to step Corpus: 000541
to stream Main, to step Curation: 000541

Le document en format XML

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<term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term>
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<term>Phosphatidylinositol 3-Kinases (genetics)</term>
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<term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Multimérisation de protéines (MeSH)</term>
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<front><div type="abstract" xml:lang="en">TOR is a serine/threonine protein kinase that assembles into distinct TOR Complexes 1 and 2 (TORC1 or TORC2) to regulate cell growth. In mammalian cells, a single mTOR incorporates stably into mTORC1 and mTORC2. By contrast, in <i>Saccharomyces cerevisiae</i>
, two highly similar Tor1 and Tor2 proteins exist, where Tor1 assembles exclusively into TORC1 and Tor2 assembles preferentially into TORC2. To gain insight into TOR complex assembly, we used this bifurcation in yeast to identify structural elements within Tor1 and Tor2 that govern their complex specificity. We have identified a concise region of ~500 amino acids within the N-terminus of Tor2, which we term the Major Assembly Specificity (MAS) domain, that is sufficient to confer significant TORC2 activity when placed into an otherwise Tor1 protein. Consistently, introduction of the corresponding MAS domain from Tor1 into an otherwise Tor2 is sufficient to confer stable association with TORC1-specific components. Remarkably, much like mTOR, this latter chimera also retains stable interactions with TORC2 components, indicating that determinants throughout Tor1/Tor2 contribute to complex specificity. Our findings are in excellent agreement with recent ultrastructural studies of TORC1 and TORC2, where the MAS domain is involved in quaternary interactions important for complex formation and/or stability.</div>
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<Abstract><AbstractText>TOR is a serine/threonine protein kinase that assembles into distinct TOR Complexes 1 and 2 (TORC1 or TORC2) to regulate cell growth. In mammalian cells, a single mTOR incorporates stably into mTORC1 and mTORC2. By contrast, in <i>Saccharomyces cerevisiae</i>
, two highly similar Tor1 and Tor2 proteins exist, where Tor1 assembles exclusively into TORC1 and Tor2 assembles preferentially into TORC2. To gain insight into TOR complex assembly, we used this bifurcation in yeast to identify structural elements within Tor1 and Tor2 that govern their complex specificity. We have identified a concise region of ~500 amino acids within the N-terminus of Tor2, which we term the Major Assembly Specificity (MAS) domain, that is sufficient to confer significant TORC2 activity when placed into an otherwise Tor1 protein. Consistently, introduction of the corresponding MAS domain from Tor1 into an otherwise Tor2 is sufficient to confer stable association with TORC1-specific components. Remarkably, much like mTOR, this latter chimera also retains stable interactions with TORC2 components, indicating that determinants throughout Tor1/Tor2 contribute to complex specificity. Our findings are in excellent agreement with recent ultrastructural studies of TORC1 and TORC2, where the MAS domain is involved in quaternary interactions important for complex formation and/or stability.</AbstractText>
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<AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California Davis, Davis, CA 95616, USA. tpowers@ucdavis.edu.</Affiliation>
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	Serveur d'exploration sur la rapamycine et les champignons
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Redesigning TOR Kinase to Explore the Structural Basis for TORC1 and TORC2 Assembly.

Redesigning TOR Kinase to Explore the Structural Basis for TORC1 and TORC2 Assembly.

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