RapamycinFungusV1, Main, Exploration, bibRecord, 000216

TORC1 specifically inhibits microautophagy through ESCRT-0.

Identifieur interne : 000216 ( Main/Exploration ); précédent : 000215; suivant : 000217

TORC1 specifically inhibits microautophagy through ESCRT-0.

Auteurs : Riko Hatakeyama [Suisse] ; Claudio De Virgilio [Suisse]

Source :

Current genetics [ 1432-0983 ] ; 2019.

RBID : pubmed:31041524

Descripteurs français

KwdFr :
- Complexe-1 cible mécanistique de la rapamycine (génétique), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Complexes de tri endosomique requis pour le transport (MeSH), Modèles biologiques (MeSH), Mutation (MeSH), Phosphorylation (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme).
MESH :

English descriptors

KwdEn :
- Endosomal Sorting Complexes Required for Transport (MeSH), Mechanistic Target of Rapamycin Complex 1 (genetics), Mechanistic Target of Rapamycin Complex 1 (metabolism), Microautophagy (genetics), Models, Biological (MeSH), Mutation (MeSH), Phosphorylation (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
MESH :
- chemical , genetics : Mechanistic Target of Rapamycin Complex 1, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Mechanistic Target of Rapamycin Complex 1, Saccharomyces cerevisiae Proteins.
- chemical : Endosomal Sorting Complexes Required for Transport.
- genetics : Microautophagy, Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Models, Biological, Mutation, Phosphorylation.

Abstract

Nutrient starvation induces the degradation of specific plasma membrane proteins through the multivesicular body (MVB) sorting pathway and of vacuolar membrane proteins through microautophagy. Both of these processes require the gateway protein Vps27, which recognizes ubiquitinated cargo proteins at phosphatidylinositol 3-phosphate-rich membranes as part of a heterodimeric complex coined endosomal sorting complex required for transport 0. The target of rapamycin complex 1 (TORC1), a nutrient-activated central regulator of cell growth, directly phosphorylates Vps27 to antagonize its function in microautophagy, but whether this also serves to restrain MVB sorting at endosomes is still an open question. Here, we show that TORC1 inhibits both the MVB pathway-driven turnover of the plasma membrane-resident high-affinity methionine permease Mup1 and the inositol transporter Itr1 and the microautophagy-dependent degradation of the vacuolar membrane-associated v-ATPase subunit Vph1. Using a Vps27^7D variant that mimics the TORC1-phosphorylated state of Vps27, we further show that cargo sorting of Vph1 at the vacuolar membrane, but not of Mup1 and Itr1 at endosomes, is sensitive to the TORC1-controlled modifications of Vps27. Thus, TORC1 specifically modulates microautophagy through phosphorylation of Vps27, but controls MVB sorting through alternative mechanisms.

DOI: 10.1007/s00294-019-00982-y
PubMed: 31041524
PubMed Central: PMC6744375

Affiliations:

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

to stream Main, to step Corpus: 000282
to stream Main, to step Curation: 000282

Le document en format XML

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<front><div type="abstract" xml:lang="en">Nutrient starvation induces the degradation of specific plasma membrane proteins through the multivesicular body (MVB) sorting pathway and of vacuolar membrane proteins through microautophagy. Both of these processes require the gateway protein Vps27, which recognizes ubiquitinated cargo proteins at phosphatidylinositol 3-phosphate-rich membranes as part of a heterodimeric complex coined endosomal sorting complex required for transport 0. The target of rapamycin complex 1 (TORC1), a nutrient-activated central regulator of cell growth, directly phosphorylates Vps27 to antagonize its function in microautophagy, but whether this also serves to restrain MVB sorting at endosomes is still an open question. Here, we show that TORC1 inhibits both the MVB pathway-driven turnover of the plasma membrane-resident high-affinity methionine permease Mup1 and the inositol transporter Itr1 and the microautophagy-dependent degradation of the vacuolar membrane-associated v-ATPase subunit Vph1. Using a Vps27<sup>7D</sup>
 variant that mimics the TORC1-phosphorylated state of Vps27, we further show that cargo sorting of Vph1 at the vacuolar membrane, but not of Mup1 and Itr1 at endosomes, is sensitive to the TORC1-controlled modifications of Vps27. Thus, TORC1 specifically modulates microautophagy through phosphorylation of Vps27, but controls MVB sorting through alternative mechanisms.</div>
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<Abstract><AbstractText>Nutrient starvation induces the degradation of specific plasma membrane proteins through the multivesicular body (MVB) sorting pathway and of vacuolar membrane proteins through microautophagy. Both of these processes require the gateway protein Vps27, which recognizes ubiquitinated cargo proteins at phosphatidylinositol 3-phosphate-rich membranes as part of a heterodimeric complex coined endosomal sorting complex required for transport 0. The target of rapamycin complex 1 (TORC1), a nutrient-activated central regulator of cell growth, directly phosphorylates Vps27 to antagonize its function in microautophagy, but whether this also serves to restrain MVB sorting at endosomes is still an open question. Here, we show that TORC1 inhibits both the MVB pathway-driven turnover of the plasma membrane-resident high-affinity methionine permease Mup1 and the inositol transporter Itr1 and the microautophagy-dependent degradation of the vacuolar membrane-associated v-ATPase subunit Vph1. Using a Vps27<sup>7D</sup>
 variant that mimics the TORC1-phosphorylated state of Vps27, we further show that cargo sorting of Vph1 at the vacuolar membrane, but not of Mup1 and Itr1 at endosomes, is sensitive to the TORC1-controlled modifications of Vps27. Thus, TORC1 specifically modulates microautophagy through phosphorylation of Vps27, but controls MVB sorting through alternative mechanisms.</AbstractText>
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TORC1 specifically inhibits microautophagy through ESCRT-0.

TORC1 specifically inhibits microautophagy through ESCRT-0.

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