The mammalian Target of Rapamycin (TOR, also known as mTOR) is an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. Rapamycin inhibits TOR activity resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. Raptor (regulatory associated protein of TOR) is a TOR-binding protein essential for TOR signaling in vivo. It acts as a TOR scaffold protein whose binding by TOR substrates is necessary for effective TOR-catalyzed phosphorylation. These substrates include the ribosomal protein S6 kinase (RP S6K) and the eukaryotic initiation factor 4E binding protein 4EBP1, proteins necessary for cell growth and proliferation and responsive to nutrient and mitogen levels. Raptor binds these proteins through a common 5 amino acid TOR-signaling (TOS) motif; mutation of this motif prevents the TOR-dependent phosphorylation of these proteins.

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