Gene interactions and pathways from curated databases and text-mining

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Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Ghosh et al., PloS one 2010 : SIRT1 negatively regulates the mammalian target of rapamycin ... Here we investigated the potential regulation of mTOR signaling by SIRT1 in response to nutrients and cellular stress ... We demonstrate that SIRT1 deficiency results in elevated mTOR signaling , which is not abolished by stress conditions ... Furthermore, we demonstrate that SIRT1 interacts with TSC2, a component of the mTOR inhibitory-complex upstream to mTORC1, and regulates mTOR signaling in a TSC2 dependent manner ... These results demonstrate that SIRT1 negatively regulates mTOR signaling potentially through the TSC1/2 complex
Back et al., J Biol Chem 2011 (Carcinoma, Squamous Cell) : Cancer cell survival following DNA damage mediated premature senescence is regulated by mammalian target of rapamycin (mTOR) dependent Inhibition of sirtuin 1 ... This process involved the mTOR dependent phosphorylation of SIRT1 at serine 47, resulting in the inhibition of the deacetylase activity of SIRT1 ... The pharmacologic and genetic inhibition of mTOR , unphosphorylatable S47A, or F474A TOS mutants restored SIRT1 deacetylase activity, blocked Bfl-1/A1 induction, and sensitized prematurely senescent SCC cells for apoptosis
Cottam et al., Autophagy 2011 (Coronavirus Infections) : The coronavirus nsp6 proteins activated omegasome and autophagosome formation independently of starvation, but activation did not involve direct inhibition of mTOR signalling, activation of sirtuin1 or induction of ER stress
Guo et al., J Neurosci Res 2011 : Coincidentally, we found that enhanced Sirt1 expression in neurons downregulated the mammalian target of rapamycin (mTOR) protein levels and its phosphorylation without changes in its mRNA levels, which was accompanied by concomitant inhibition of the mTOR downstream signaling activity as revealed by decreased p70S6 kinase (p70S6K) phosphorylation at Thr389. Consistently with this, using a Sirt1 siRNA transfection approach, we observed that reduction of endogenous mouse Sirt1 led to increased levels of mTOR and phosphorylation of itself and p70S6K as well as impaired cell survival and neurite outgrowth in wild-type mouse primary neurons, corroborating a suppressing effect of mTOR by Sirt1