Gene interactions and pathways from curated databases and text-mining

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AKT1 — TSC2

Pathways - manually collected, often from reviews:

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

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Potter et al., Nat Cell Biol 2002 : Akt regulates growth by directly phosphorylating Tsc2 ... Stimulating Akt/PKB signalling in vivo markedly increases cell growth/size, disrupts the Tsc1-Tsc2 complex and disturbs the distinct subcellular localization of Tsc1 and Tsc2
Potter et al., Biochem Soc Trans 2003 : We have shown that Akt regulates the Tsc1-Tsc2 complex by directly phosphorylating Tsc2 ... We have shown that Akt regulates the Tsc1-Tsc2 complex by directly phosphorylating Tsc2
Hahn-Windgassen et al., J Biol Chem 2005 : Here we establish an additional pathway by which Akt inhibits TSC2 and activates mTOR ... Currently, the Akt mediated phosphorylation of TSC2 and the inhibition of AMPK mediated phosphorylation of TSC2 are viewed as two separate pathways, which activate mTOR ... Our results demonstrate that Akt lies upstream of these two pathways and induces full inhibition of TSC2 and activation of mTOR both through direct phosphorylation and by inhibition of AMPK mediated phosphorylation of TSC2
Kayampilly et al., Endocrinology 2007 (MAP Kinase Signaling System) : Because Akt is the upstream activator of TSC2 phosphorylation, the effect of Akt inhibition was examined to test whether FSH mediated TSC2 phosphorylation proceeds through an Akt dependent pathway ... These results demonstrate the involvement of ERK rather than Akt in FSH mediated TSC2 phosphorylation in granulosa cells
Vojtechová et al., Neoplasia (New York, N.Y.) 2008 : The ectopic, active Akt1 that was expressed in Src-deficient cells significantly enhanced phosphorylation of TSC2 in these cells, but it failed to activate the inhibited components of the mTOR pathway that are downstream of TSC2
Dan et al., J Immunol 2008 : mTOR is negatively controlled by the tuberous sclerosis complex 1/2 (TSC1/2), and activation of Akt induces phosphorylation of TSC2 , which blocks the repressive TSC1/2 activity
Huang et al., Biochem Soc Trans 2009 : Akt/PKB ( protein kinase B ) both regulates and is regulated by the TSC ( tuberous sclerosis complex ) 1-TSC2 complex ... Akt/PKB ( protein kinase B ) both regulates and is regulated by the TSC ( tuberous sclerosis complex ) 1-TSC2 complex
Codeluppi et al., J Neurosci 2009 (Disease Models, Animal...) : This occurs through Akt mediated phosphorylation of the GTPase activating protein Tuberin , which inhibits Tuberin 's ability to inactivate the small GTPase Rheb
Pollizzi et al., Molecular cancer 2009 (Disease Models, Animal...) : Loss of either TSC1 or TSC2 in TSC hamartomas leads to activation of mTORC1 and suppression of AKT
Zhang et al., PloS one 2009 : Loss of function of the TSC1-TSC2 complex results in constitutive mTORC1 signaling and, through mTORC1 dependent feedback mechanisms and loss of mTORC2 activity, leads to a concomitant block of Akt signaling to its other downstream targets
Blancquaert et al., Mol Endocrinol 2010 : Unlike insulin, TSH/cAMP did not activate protein kinase B or induce tuberous sclerosis complex 2 phosphorylation at T1462 and Y1571
Hwang et al., BMB Rep 2011 (Ischemia) : The loss of TSC2 , which is upstream of mTOR, activates S6K1, promotes cell growth and survival, activates mTOR kinase activities, inhibits mTORC1 and mTORC2 via mTOR inhibitors, and suppresses S6K1 and Akt
Das et al., J Biol Chem 2012 (Tuberous Sclerosis) : TSC2 deficiency induces constitutive activation of mTOR, leading to a state of insulin resistance due to a negative feedback regulation, resulting in reduced Akt phosphorylation
Zurashvili et al., Mol Cell Biol 2013 : In contrast, PKB mediated phosphorylation of PRAS40 and TSC2 , allowing optimal mTORC1 activation and brain-specific kinase (BRSK) protein synthesis, was markedly reduced in the mutant mice, leading to impaired neuronal growth and differentiation