RapamycinFungusV1, Main, Exploration, bibRecord, 000721

The Architecture of the Rag GTPase Signaling Network.

Identifieur interne : 000721 ( Main/Exploration ); précédent : 000720; suivant : 000722

The Architecture of the Rag GTPase Signaling Network.

Auteurs : Raffaele Nicastro [Suisse] ; Alessandro Sardu [Suisse] ; Nicolas Panchaud [Suisse] ; Claudio De Virgilio [Suisse]

Source :

Biomolecules [ 2218-273X ] ; 2017.

RBID : pubmed:28788436

Descripteurs français

KwdFr :
- Acides aminés (métabolisme), Animaux (MeSH), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Humains (MeSH), Levures (métabolisme), Modèles moléculaires (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme), Régulation de l'expression des gènes (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Transduction du signal (MeSH), dGTPases (composition chimique), dGTPases (métabolisme).
MESH :
- composition chimique : Protéines fongiques, dGTPases.
- métabolisme : Acides aminés, Complexe-1 cible mécanistique de la rapamycine, Levures, Protéines fongiques, dGTPases.
- Animaux, Humains, Modèles moléculaires, Régulation de l'expression des gènes, Séquence conservée, Séquence d'acides aminés, Transduction du signal.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (metabolism), Animals (MeSH), Conserved Sequence (MeSH), Fungal Proteins (chemistry), Fungal Proteins (metabolism), GTP Phosphohydrolases (chemistry), GTP Phosphohydrolases (metabolism), Gene Expression Regulation (MeSH), Humans (MeSH), Mechanistic Target of Rapamycin Complex 1 (metabolism), Models, Molecular (MeSH), Signal Transduction (MeSH), Yeasts (metabolism).
MESH :
- chemical , chemistry : Fungal Proteins, GTP Phosphohydrolases.
- chemical , metabolism : Amino Acids, Fungal Proteins, GTP Phosphohydrolases, Mechanistic Target of Rapamycin Complex 1.
- metabolism : Yeasts.
- Amino Acid Sequence, Animals, Conserved Sequence, Gene Expression Regulation, Humans, Models, Molecular, Signal Transduction.

Abstract

The evolutionarily conserved target of rapamycin complex 1 (TORC1) couples an array of intra- and extracellular stimuli to cell growth, proliferation and metabolism, and its deregulation is associated with various human pathologies such as immunodeficiency, epilepsy, and cancer. Among the diverse stimuli impinging on TORC1, amino acids represent essential input signals, but how they control TORC1 has long remained a mystery. The recent discovery of the Rag GTPases, which assemble as heterodimeric complexes on vacuolar/lysosomal membranes, as central elements of an amino acid signaling network upstream of TORC1 in yeast, flies, and mammalian cells represented a breakthrough in this field. Here, we review the architecture of the Rag GTPase signaling network with a special focus on structural aspects of the Rag GTPases and their regulators in yeast and highlight both the evolutionary conservation and divergence of the mechanisms that control Rag GTPases.

DOI: 10.3390/biom7030048
PubMed: 28788436
PubMed Central: PMC5618229

Affiliations:

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

to stream Main, to step Corpus: 000755
to stream Main, to step Curation: 000755

Le document en format XML

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<term>Conserved Sequence (MeSH)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (metabolism)</term>
<term>GTP Phosphohydrolases (chemistry)</term>
<term>GTP Phosphohydrolases (metabolism)</term>
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<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Levures (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Régulation de l'expression des gènes (MeSH)</term>
<term>Séquence conservée (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Transduction du signal (MeSH)</term>
<term>dGTPases (composition chimique)</term>
<term>dGTPases (métabolisme)</term>
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<term>Mechanistic Target of Rapamycin Complex 1</term>
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<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Levures</term>
<term>Protéines fongiques</term>
<term>dGTPases</term>
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<term>Conserved Sequence</term>
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<term>Signal Transduction</term>
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<term>Humains</term>
<term>Modèles moléculaires</term>
<term>Régulation de l'expression des gènes</term>
<term>Séquence conservée</term>
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<front><div type="abstract" xml:lang="en">The evolutionarily conserved target of rapamycin complex 1 (TORC1) couples an array of intra- and extracellular stimuli to cell growth, proliferation and metabolism, and its deregulation is associated with various human pathologies such as immunodeficiency, epilepsy, and cancer. Among the diverse stimuli impinging on TORC1, amino acids represent essential input signals, but how they control TORC1 has long remained a mystery. The recent discovery of the Rag GTPases, which assemble as heterodimeric complexes on vacuolar/lysosomal membranes, as central elements of an amino acid signaling network upstream of TORC1 in yeast, flies, and mammalian cells represented a breakthrough in this field. Here, we review the architecture of the Rag GTPase signaling network with a special focus on structural aspects of the Rag GTPases and their regulators in yeast and highlight both the evolutionary conservation and divergence of the mechanisms that control Rag GTPases.</div>
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<Abstract><AbstractText>The evolutionarily conserved target of rapamycin complex 1 (TORC1) couples an array of intra- and extracellular stimuli to cell growth, proliferation and metabolism, and its deregulation is associated with various human pathologies such as immunodeficiency, epilepsy, and cancer. Among the diverse stimuli impinging on TORC1, amino acids represent essential input signals, but how they control TORC1 has long remained a mystery. The recent discovery of the Rag GTPases, which assemble as heterodimeric complexes on vacuolar/lysosomal membranes, as central elements of an amino acid signaling network upstream of TORC1 in yeast, flies, and mammalian cells represented a breakthrough in this field. Here, we review the architecture of the Rag GTPase signaling network with a special focus on structural aspects of the Rag GTPases and their regulators in yeast and highlight both the evolutionary conservation and divergence of the mechanisms that control Rag GTPases.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nicastro</LastName>
<ForeName>Raffaele</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland. raffaele.nicastro2@unifr.ch.</Affiliation>
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<ForeName>Alessandro</ForeName>
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<ForeName>Nicolas</ForeName>
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	Serveur d'exploration sur la rapamycine et les champignons
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The Architecture of the Rag GTPase Signaling Network.

The Architecture of the Rag GTPase Signaling Network.

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