XPLN is an endogenous inhibitor of mTORC2.

ABSTRACT: Mammalian target of rapamycin complex 2 (mTORC2) controls a wide range of cellular and developmental processes, but its regulation remains incompletely understood. Through a yeast two-hybrid screen, we have identified XPLN (exchange factor found in platelets, leukemic, and neuronal tissues), a guanine nucleotide exchange factor (GEF) for Rho GTPases, as an interacting partner of mTOR. In mammalian cells, XPLN interacts with mTORC2 but not with mTORC1, and this interaction is dependent on rictor. Knockdown of XPLN enhances phosphorylation of the Ser/Thr kinase Akt, a target of mTORC2, whereas overexpression of XPLN suppresses it, suggesting that XPLN inhibits mTORC2 signaling to Akt. Consistent with Akt promoting cell survival and XPLN playing a negative role in this process, XPLN knockdown

SUBMITTER: Khanna N 

PROVIDER: S-EPMC3791717 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature