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 inhibits TSC1 bound to TSC2. 2 / 2
2 |
signor
"We have shown thataktregulates the tsc1-tsc2 complex by directly phosphorylating tsc2. Tsc2 is inactivated by akt-dependent phosphorylation, which destabilizes tsc2 and disrupts its interaction with tsc1. Tsc2 is inactivated by akt-dependent phosphorylation, which destabilizes tsc2 and disrupts its interaction with tsc1akt has been shown to directly phosphorylate two sites on tsc2 (s939 and t1462 on the full-length human protein), which are conserved and phosphorylated in drosophila tsc2, and is likely to phosphorylate two or three additional sites (s981 and s1130/s1132)."
signor
"In examining the requirements for different Akt-mediated phosphorylation sites on TSC2, we find that only TSC2 mutants lacking all five previously identified Akt sites fully block insulin-stimulated mTORC1 signaling in reconstituted Tsc2 null cells, and this mutant also inhibits adipogenesis"
Kinase-active AKT1 inhibits TSC1 bound to TSC2. 1 / 1
1 |
bel
"In turn, Akt phosphorylates the tuberous scleorisis complex, TSC1/TSC2 (hamartin/tuberin) that serves as a GTPase activating protein (GAP) for the small G protein, Ras homolog enriched in brain (Rheb)."
AKT1 inhibits TSC1. 1 / 1
| 1
reach
"Akt1 dependent phosphorylation negatively regulates the functioning of TSC1 and TSC2, 2 other factors involved in insulin signaling."