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TORC2 controls endocytosis through plasma membrane tension.

  • Riggi M Department of Molecular Biology, University of Geneva, Geneva, Switzerland.
  • Bourgoint C Department of Molecular Biology, University of Geneva, Geneva, Switzerland.
  • Macchione M Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.
  • Matile S Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.
  • Loewith R Department of Molecular Biology, University of Geneva, Geneva, Switzerland robbie.loewith@unige.ch.
  • Roux A Department of Biochemistry, University of Geneva, Geneva, Switzerland aurelien.roux@unige.ch.
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  • 2019-05-25
Published in:
  • The Journal of cell biology. - 2019
Actin Cytoskeleton
Cell Membrane
Cytoplasm
Cytoskeletal Proteins
Endocytosis
Mechanistic Target of Rapamycin Complex 2
Microfilament Proteins
Phosphorylation
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Signal Transduction
Vesicular Transport Proteins
English 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.
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  • English
Open access status
gold
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Persistent URL
https://sonar.ch/global/documents/133986
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