Mechanistic Target of Rapamycin Kinase (mTOR)

mTOR is a 289-kDa serine-threonine kinase that serves as a central regulator of cellular processes. It forms the catalytic subunit of two distinct multi-protein complexes, mTORC1 and mTORC2, which integrate both intracellular and extracellular signals to regulate cell metabolism, growth, proliferation, and survival. mTORC1 consists of mTOR, Raptor, mLST8, PRAS40, and Deptor, while mTORC2 has a different composition. mTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. The mTOR signaling pathway is evolutionarily conserved and plays crucial roles in brain development and function, particularly in synaptic plasticity. Dysregulation of mTOR signaling has been implicated in various diseases, including cancer, neurological disorders, and metabolic diseases, making it an important therapeutic target.

Other names

Mammalian Target of RapamycinFK506-binding protein 12-rapamycin-associated protein 1FKBP-rapamycin associated proteinFKBP12-rapamycin complex-associated protein 1FRAP2RAFT1Rapamycin and FKBP12 target 1Rapamycin target protein 1RAPT1Serine/threonine-protein kinase mTOR

mTOR functions through two distinct protein complexes: mTOR Complex 1 (mTORC1) and mTOR Complex 2 (mTORC2). mTORC1 regulates protein synthesis, cell growth, and metabolism, while mTORC2 regulates cell survival, cytoskeleton organization, and activates AKT signaling. mTOR inhibitors like rapamycin work by binding to FKBP12 and forming a complex that inhibits mTOR activity.