UNIGE document Scientific Article
previous document  unige:103222  next document
add to browser collection
Title

TORC2 Structure and Function

Authors
Published in Trends in Biochemical Sciences. 2016, vol. 41, no. 6, p. 532-545
Abstract The target of rapamycin (TOR) kinase functions in two multiprotein complexes, TORC1 and TORC2. Although both complexes are evolutionarily conserved, only TORC1 is acutely inhibited by rapamycin. Consequently, only TORC1 signaling is relatively well understood; and, at present, only mammalian TORC1 is a validated drug target, pursued in immunosuppression and oncology. However, the knowledge void surrounding TORC2 is dissipating. Acute inhibition of TORC2 with small molecules is now possible and structural studies of both TORC1 and TORC2 have recently been reported. Here we review these recent advances as well as observations made from tissue-specific mTORC2 knockout mice. Together these studies help define TORC2 structure-function relationships and suggest that mammalian TORC2 may one day also become a bona fide clinical target.
Keywords AnimalsAntibioticsAntineoplastic/pharmacologyBinding SitesGene Expression RegulationHumansMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2MiceMiceKnockoutModelsMolecularMultiprotein Complexes/antagonists & inhibitors/chemistry/genetics/metabolismProtein BindingProtein ConformationAlpha-HelicalProtein Interaction Domains and MotifsProtein Subunits/chemistry/genetics/metabolismSignal TransductionSirolimus/pharmacologyStructure-Activity RelationshipTOR Serine-Threonine Kinases/antagonists & inhibitors/chemistry/genetics/metabolism
Identifiers
PMID: 27161823
Full text
Article (Published version) (2.9 MB) - document accessible for UNIGE members only Limited access to UNIGE
Structures
Research group Groupe Loewith
Citation
(ISO format)
GAUBITZ, Christl et al. TORC2 Structure and Function. In: Trends in Biochemical Sciences, 2016, vol. 41, n° 6, p. 532-545. https://archive-ouverte.unige.ch/unige:103222

8 hits

0 download

Update

Deposited on : 2018-03-27

Export document
Format :
Citation style :