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TORC2 controls endocytosis through plasma membrane tension.

Identifieur interne : 000214 ( Main/Exploration ); précédent : 000213; suivant : 000215

TORC2 controls endocytosis through plasma membrane tension.

Auteurs : Margot Riggi [Suisse] ; Clélia Bourgoint [Suisse] ; Mariano Macchione [Suisse] ; Stefan Matile [Suisse] ; Robbie Loewith [Suisse] ; Aurélien Roux [Suisse]

Source :

RBID : pubmed:31123183

Descripteurs français

English descriptors

Abstract

Target of rapamycin complex 2 (TORC2) is a conserved protein kinase that regulates multiple plasma membrane (PM)-related processes, including endocytosis. Direct, chemical inhibition of TORC2 arrests endocytosis but with kinetics that is relatively slow and therefore inconsistent with signaling being mediated solely through simple phosphorylation cascades. Here, we show that in addition to and independently from regulation of the phosphorylation of endocytic proteins, TORC2 also controls endocytosis by modulating PM tension. Elevated PM tension, upon TORC2 inhibition, impinges on endocytosis at two different levels by (1) severing the bonds between the PM adaptor proteins Sla2 and Ent1 and the actin cytoskeleton and (2) hindering recruitment of Rvs167, an N-BAR-containing protein important for vesicle fission to endocytosis sites. These results underline the importance of biophysical cues in the regulation of cellular and molecular processes.

DOI: 10.1083/jcb.201901096
PubMed: 31123183
PubMed Central: PMC6605812


Affiliations:


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Le document en format XML

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<term>Cytoplasm (genetics)</term>
<term>Cytoskeletal Proteins (genetics)</term>
<term>Endocytosis (genetics)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (genetics)</term>
<term>Microfilament Proteins (genetics)</term>
<term>Phosphorylation (MeSH)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
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<term>Complexe-2 cible mécanistique de la rapamycine (génétique)</term>
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<term>Membrane cellulaire (génétique)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines des microfilaments (génétique)</term>
<term>Protéines du cytosquelette (génétique)</term>
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<term>Mechanistic Target of Rapamycin Complex 2</term>
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<term>Cell Membrane</term>
<term>Cytoplasm</term>
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<term>Signal Transduction</term>
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<term>Complexe-2 cible mécanistique de la rapamycine</term>
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<div type="abstract" xml:lang="en">Target of rapamycin complex 2 (TORC2) is a conserved protein kinase that regulates multiple plasma membrane (PM)-related processes, including endocytosis. Direct, chemical inhibition of TORC2 arrests endocytosis but with kinetics that is relatively slow and therefore inconsistent with signaling being mediated solely through simple phosphorylation cascades. Here, we show that in addition to and independently from regulation of the phosphorylation of endocytic proteins, TORC2 also controls endocytosis by modulating PM tension. Elevated PM tension, upon TORC2 inhibition, impinges on endocytosis at two different levels by (1) severing the bonds between the PM adaptor proteins Sla2 and Ent1 and the actin cytoskeleton and (2) hindering recruitment of Rvs167, an N-BAR-containing protein important for vesicle fission to endocytosis sites. These results underline the importance of biophysical cues in the regulation of cellular and molecular processes.</div>
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<AbstractText>Target of rapamycin complex 2 (TORC2) is a conserved protein kinase that regulates multiple plasma membrane (PM)-related processes, including endocytosis. Direct, chemical inhibition of TORC2 arrests endocytosis but with kinetics that is relatively slow and therefore inconsistent with signaling being mediated solely through simple phosphorylation cascades. Here, we show that in addition to and independently from regulation of the phosphorylation of endocytic proteins, TORC2 also controls endocytosis by modulating PM tension. Elevated PM tension, upon TORC2 inhibition, impinges on endocytosis at two different levels by (1) severing the bonds between the PM adaptor proteins Sla2 and Ent1 and the actin cytoskeleton and (2) hindering recruitment of Rvs167, an N-BAR-containing protein important for vesicle fission to endocytosis sites. These results underline the importance of biophysical cues in the regulation of cellular and molecular processes.</AbstractText>
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