Direct physical interaction of active Ras with mSIN1 regulates mTORC2 signaling.

ABSTRACT:

Background

The mechanistic (or mammalian) target of rapamycin (mTOR), a Ser/Thr kinase, associates with different subunits forming two functionally distinct complexes, mTORC1 and mTORC2, regulating a diverse set of cellular functions in response to growth factors, cellular energy levels, and nutrients. The mechanisms regulating mTORC1 activity are well characterized; regulation of mTORC2 activity, however, remains obscure. While studies conducted in Dictyostelium suggest a possible role of Ras protein as a potential upstream regulator of mTORC2, definitive studies delineating the underlying molecular mechanisms, particularly in mammalian cells, are still lacking.

Methods

Protein levels were measured by Western blotting and kinase activity of mTORC2 was analyzed by in vitro k

SUBMITTER: Lone MU 

PROVIDER: S-EPMC6921532 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature