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Structural basis for TORC2 activation.

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Summary
This summary is machine-generated.

Target of rapamycin complex 2 (TORC2) maintains plasma membrane (PM) homeostasis. This study reveals TORC2

Keywords:
TOR signalingcell growthcryo-electron microscopymembrane mechanotransductionphosphoinositidestarget of rapamycin complex 2

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Area of Science:

  • Cellular signaling
  • Molecular biology
  • Structural biology

Background:

  • The target of rapamycin complex 2 (TORC2) is crucial for maintaining plasma membrane (PM) biophysical homeostasis.
  • Regulation of TORC2 by mechanical stress on the PM remains poorly understood.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying TORC2 regulation, particularly in response to mechanical perturbations.
  • To provide a high-resolution structural model of endogenous yeast TORC2.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of yeast TORC2.
  • Structure-guided functional experiments to validate regulatory mechanisms.

Main Results:

  • Determined the cryo-EM structure of yeast TORC2 at 2.2 Å resolution, refining subunit interactions.
  • Observed the Avo1 subunit's pleckstrin-homology domain interacting with the Tor2 active site, suggesting phosphoinositide-mediated regulation.
  • Identified a potential TORC2 membrane-binding surface and a key positively charged pocket in Avo3 required for activation.

Conclusions:

  • Signaling phosphoinositides activate TORC2 through membrane-induced structural changes.
  • Conserved regulatory subunits play a concerted role in TORC2 activation via structural rearrangements.