mTOR complex 1 (mTORC1) and mTORC2 integrate upstream environmental
information to gate their own activation. Because mTORC1 controls cellular entry
into an anabolic state that requires copious amounts of energy and
macromolecules, activation of the complex should only occur when amino acids,
insulin/growth factors, ATP and oxygen are all readily available. To ensure that
all of these requirements are satisfied, mTORC1 must translocate to the lysosome
by anchoring onto the Rag GTPases, which are only competent to recruit mTORC1 in
the presence of amino acids. Once localized to the lysosomal surface, mTORC1 can
be then be activated by the small GTPase Rheb in its GTP-bound state.
Importantly, GTP loading of Rheb is promoted by growth factors and opposed by
energetic stress or hypoxia. All of these inputs converge on tuberous sclerosis
complex (TSC), which acts as a GAP for Rheb. mTORC2 is thought to be primarily
regulated by growth factors. Although it is not clear where mTORC2 activation
occurs, the pleckstrin homology domain on MAPK-interacting protein 1 (mSIN1) may
recruit mTORC2 to the plasma membrane. Positive regulators of the mTORC1 pathway
are shown in green, while negative regulators of mTORC1 are shown in blue. AMPK,
AMP-activated protein kinase; CASTOR, cellular arginine sensor for mTORC1; EGFR,
epidermal growth factor receptor; FLCN, folliculin; GATOR, GAP activity towards
the Rags; Grb2, growth factor receptor-bound protein 2; GSK3, glycogen synthase
kinase 3; IGF, insulin-like growth factor; IKKβ, inhibitor of nuclear
factor κB kinase β; IRS, insulin receptor substrate; LKB1, liver
kinase B1; Mek, MAPK/ERK kinase; NF1, neurofibromatosis type 1; PIP2,
phosphatidylinositol (4,5)-bisphosphate; PIP3, phosphatidylinositol
(3,4,5)-trisphosphate; PTEN, phosphatase and tensin homologue; RSK, p90
ribosomal S6 kinase; SAM, S-adenosylmethionine; SAMTOR,
S-adenosylmethionine sensor; Sos, son of sevenless; TNF,
tumour necrosis factor.