Feb 6, 2017
Localizing mTORC2 activity
The mTORC2 complex regulates cell growth and proliferation by phosphorylating the protein kinase Akt, but where in the cell mTORC2 is active, and how growth factors direct its activity towards Akt, remains unclear. Ebner et al. use a novel reporter to show that endogenous mTORC2 activity localizes to plasma membrane, mitochondrial, and endosomal pools with distinct sensitivities to PI3 kinase and growth factor signaling, and that growth factors induce Akt phosphorylation by promoting Akt's recruitment to the plasma membrane. This biosights episode presents the paper by Ebner et al. from the February 6th, 2017, issue of The Journal of Cell Biology and includes an interview with two of the paper's authors, Michael Ebner and Ivan Yudushkin (Max F. Perutz Laboratories and Medical University of Vienna, Vienna, Austria). Produced by Caitlin Sedwick and Ben Short. See the associated paper in JCB for details on the funding provided to support this original research.
The Rockefeller University Press