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MTOR — SIRT1
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