A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

IndraLab

Statements

databases
phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
reading

AKT1 phosphorylates MTOR on S2448. 10 / 10
1 1 3 | 3 2
reach
"mTOR is phosphorylated by Akt1 at Ser2448, leading to downstream signaling by p-mTOR."
sparser
"Activated mTOR is phosphorylated at Ser 2448 by AKT1 and functions in mediating cell growth and proliferation [16] ."
hprd
No evidence text available
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 "
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."
biopax:phosphositeplus
No evidence text available
sparser
"mTOR is phosphorylated by Akt1 at Ser2448, leading to downstream signaling by p-mTOR. xref The premise of our study was to examine the regulatory relationship between the mTOR pathway and PKM2."
hprd
No evidence text available
hprd
No evidence text available
signor
"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."