The mammalian target of rapamycin (mTOR) is a major effector of cell growth and proliferation via the regulation of protein synthesis. mTOR is composed of an N-terminal half of 20 tandem HEAT repeats that are implicated in protein-protein interactions and a C-terminal half that includes a FAT domain, a FBR domain, a kinase domain, a NDR domain and a FATC domain. The FATC domain is essential to mTOR activity, and the deletion of a single amino acid from this domain abrogates this activity. mTOR can be auto-phosphorylated via its intrinsic serine/threonine kinase activity. mTOR regulates protein synthesis through the phosphorylation and inactivation of the mRNA translation repressor, 4E-BP1, and also through the phosphorylation and activation of S6 kinase. RAPTOR (regulatory associated protein of TOR) is a positive regulator of TOR. Moreover, other known mediators of mTOR include PI3-K and ATK from the insulin pathway.
Senescence and Autophagy
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