RapamycinFungusV1, Main, Exploration, bibRecord, 001375

Tor directly controls the Atg1 kinase complex to regulate autophagy.

Identifieur interne : 001375 ( Main/Exploration ); précédent : 001374; suivant : 001376

Tor directly controls the Atg1 kinase complex to regulate autophagy.

Auteurs : Yoshiaki Kamada [Japon] ; Ken-Ichi Yoshino ; Chika Kondo ; Tomoko Kawamata ; Noriko Oshiro ; Kazuyoshi Yonezawa ; Yoshinori Ohsumi

Source :

Molecular and cellular biology [ 1098-5549 ] ; 2010.

RBID : pubmed:19995911

Descripteurs français

KwdFr :
- Autophagie (MeSH), Données de séquences moléculaires (MeSH), Liaison aux protéines (MeSH), Microscopie électronique (MeSH), Phosphorylation (MeSH), Protein kinases (composition chimique), Protein kinases (génétique), Protein kinases (métabolisme), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines associées à l'autophagie (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Séquence d'acides aminés (MeSH).
MESH :
- composition chimique : Protein kinases, Protéines de Saccharomyces cerevisiae.
- cytologie : Saccharomyces cerevisiae.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Protein kinases, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Protein kinases, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae.
- Autophagie, Données de séquences moléculaires, Liaison aux protéines, Microscopie électronique, Phosphorylation, Protéines associées à l'autophagie, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Autophagy (MeSH), Autophagy-Related Proteins (MeSH), Microscopy, Electron (MeSH), Molecular Sequence Data (MeSH), Phosphorylation (MeSH), Protein Binding (MeSH), Protein Kinases (chemistry), Protein Kinases (genetics), Protein Kinases (metabolism), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
MESH :
- chemical , chemistry : Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Protein Kinases, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Protein Kinases, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- chemical : Autophagy-Related Proteins.
- cytology : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- Amino Acid Sequence, Autophagy, Microscopy, Electron, Molecular Sequence Data, Phosphorylation, Protein Binding.

Abstract

Autophagy is a bulk proteolytic process that is indispensable for cell survival during starvation. Autophagy is induced by nutrient deprivation via inactivation of the rapamycin-sensitive Tor complex1 (TORC1), a protein kinase complex regulating cell growth in response to nutrient conditions. However, the mechanism by which TORC1 controls autophagy and the direct target of TORC1 activity remain unclear. Atg13 is an essential regulatory component of autophagy upstream of the Atg1 kinase complex, and here we show that yeast TORC1 directly phosphorylates Atg13 at multiple Ser residues. Additionally, expression of an unphosphorylatable Atg13 mutant bypasses the TORC1 pathway to induce autophagy through activation of Atg1 in cells growing under nutrient-rich conditions. Our findings suggest that the direct control of the Atg1 complex by TORC1 induces autophagy.

DOI: 10.1128/MCB.01344-09
PubMed: 19995911
PubMed Central: PMC2815578

Affiliations:

Japon

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

to stream Main, to step Corpus: 001458
to stream Main, to step Curation: 001458

Le document en format XML

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<front><div type="abstract" xml:lang="en">Autophagy is a bulk proteolytic process that is indispensable for cell survival during starvation. Autophagy is induced by nutrient deprivation via inactivation of the rapamycin-sensitive Tor complex1 (TORC1), a protein kinase complex regulating cell growth in response to nutrient conditions. However, the mechanism by which TORC1 controls autophagy and the direct target of TORC1 activity remain unclear. Atg13 is an essential regulatory component of autophagy upstream of the Atg1 kinase complex, and here we show that yeast TORC1 directly phosphorylates Atg13 at multiple Ser residues. Additionally, expression of an unphosphorylatable Atg13 mutant bypasses the TORC1 pathway to induce autophagy through activation of Atg1 in cells growing under nutrient-rich conditions. Our findings suggest that the direct control of the Atg1 complex by TORC1 induces autophagy.</div>
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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 directly controls the Atg1 kinase complex to regulate autophagy.

Tor directly controls the Atg1 kinase complex to regulate autophagy.

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