IndraLab
Statements
"Although AKT phosphorylated mTOR at two COOH-terminal sites (Thr2446 and Ser2448) in vitro, Ser2448 was the major phosphorylation site in insulin-stimulated or -activated AKT-expressing human embryonic kidney cells. Transient transfection assays with mTOR mutants bearing Ala substitutions at Ser2448 and/or Thr2446 indicated that AKT-dependent mTOR phosphorylation was not essential for either PHAS-I phosphorylation or p70S6K activation in HEK cells."
reach
"Despite modulation of PRAS40, which regulates the mTOR containing TORC1 complex, mutational activation of PIK3CA or AKT1 did not consistently increase phosphorylation of mTOR at serine 2448 or phosphorylation of mTOR target proteins and their targets, including p70-ribosomal protein S6-kinase (p70S6K), eukaryotic elongation factor 4 binding protein 1 (EIF4EBP1), and ribosomal protein S6."
sparser
"The mTORC1 is acutely inhibited by rapamycin, which has been used therapeutically and experimentally as a probe to gain insight into mTORC1 regulation and function. xref The mTORC2 is significantly less sensitive to rapamycin than mTORC1. xref mTORC1 is known to suppress autophagy, which is a key catabolic process. xref The mTOR is phosphorylated by Akt1 at Ser2448 to yield phospho-mTOR (p-mTOR), which regulates ribosome biogenesis and protein synthesis, xref and is also present in the cytoplasm and nucleus, with high p-mTOR expression indicating reduced response to tumor treatment. xref , xref "