Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for TORC2 activation.
Journal, issue, pages	Mol Cell, Vol. 86, Issue 8, Page 1560-11573.e5, Year 2026
Publish date	Apr 16, 2026
Authors	Luoming Zou / Maria G Tettamanti / Caroline Gabus / Ariane Bergmann / Robbie Loewith / Lucas Tafur /
PubMed Abstract	The target of rapamycin complex 2 (TORC2) is a central node in signaling feedback loops, serving to maintain the biophysical homeostasis of the plasma membrane (PM). How TORC2 is regulated by ...The target of rapamycin complex 2 (TORC2) is a central node in signaling feedback loops, serving to maintain the biophysical homeostasis of the plasma membrane (PM). How TORC2 is regulated by mechanical perturbation of the PM is not well understood. To address this, we determined the cryo-electron microscopy structure of endogenous yeast TORC2 at up to 2.2 Å resolution. Our model refines the position and interactions of TORC2-specific subunits, providing a structural basis for the differential assembly of Tor2 into TORC2. Furthermore, we observe the insertion of the pleckstrin-homology domain of the Avo1 subunit into the Tor2 active site, providing a regulatory mechanism mediated by phosphoinositides. Structure-guided functional experiments reveal a potential TORC2 membrane-binding surface and a positively charged pocket in the Avo3 subunit that is necessary for TORC2 activation. Collectively, our data suggest that signaling phosphoinositides activate TORC2 by membrane-induced structural rearrangements via the concerted action of conserved regulatory subunits.
External links	Mol Cell / PubMed:41997113
Methods	EM (single particle)
Resolution	2.2 - 3.83 Å
Structure data	54222 9rsq EMDB-54222, PDB-9rsq: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) with the Avo1 PH domain (monomer) Method: EM (single particle) / Resolution: 3.07 Å 54223 9rss EMDB-54223, PDB-9rss: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) with the Avo1 PH domain Method: EM (single particle) / Resolution: 3.01 Å 54224 9rst EMDB-54224, PDB-9rst: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) in autoinhibted conformation (monomer) Method: EM (single particle) / Resolution: 2.93 Å EMDB-54227: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) (consensus refinement) Method: EM (single particle) / Resolution: 2.4 Å EMDB-54228: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) (monomer focused) Method: EM (single particle) / Resolution: 2.32 Å EMDB-54229: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) (Avo3 focused) Method: EM (single particle) / Resolution: 2.2 Å EMDB-54230: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) (Bit61 focused) Method: EM (single particle) / Resolution: 2.7 Å EMDB-54231: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) with Avo1 PH (Lst8 monomer focused) Method: EM (single particle) / Resolution: 3.0 Å EMDB-54232: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) in autoinhibited conformation (monomer Lst8 focused) Method: EM (single particle) / Resolution: 3.1 Å EMDB-54233: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) (Lst8-Avo1 CRIM focused) Method: EM (single particle) / Resolution: 3.83 Å EMDB-54234: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) with the Avo1 PH domain (composite map) Method: EM (single particle) / Resolution: 3.07 Å EMDB-54235: Cryo-EM structure of the Target of Rapamycin Complex 2 (TORC2) in autoinhibited conformation (composite map) Method: EM (single particle) / Resolution: 2.93 Å
Chemicals	ChemComp-IHP: INOSITOL HEXAKISPHOSPHATE
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	SIGNALING PROTEIN / Cell growth / metabolism