Gene interactions and pathways from curated databases and text-mining

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AKT2 — PPP2R1A

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Yung et al., J Neurochem 2003 : The PP1/PP2A phosphatase inhibitors okadaic acid and caliculyn A, but not cyclosporine A, delayed the removal of ERK and Akt phosphorylation under OGD
Li et al., Mol Cell Biol 2003 (Prostatic Neoplasms) : Analysis of potential substrates for PP1 and PP2A revealed that cav-1 mediated inhibition of PP1 and PP2A leads to increased PDK1, Akt , and ERK1/2 activities
Zuluaga et al., Cell Signal 2007 : Negative regulation of Akt activity by p38alpha MAP kinase in cardiomyocytes involves membrane localization of PP2A through interaction with caveolin-1
Ni et al., Proc Natl Acad Sci U S A 2007 (Insulin Resistance) : Repression of Akt-PP2A/B interactions and phosphatase activities contributes , at least in part, to FoxO dependent increases in Akt phosphorylation and kinase activity
Guénin et al., Int J Oncol 2008 (Melanoma, Experimental) : Protein phosphatase 2A (PP2A) , an Akt pathway inhibitor , is considered to be activated by methylation of its catalytic subunit ... In untreated cells, okadaic acid, an antagonist of PP2A methylation, inhibited PP2A activity, stimulated cell proliferation, increased Akt activation and c-Myc expression
Modak et al., Biochem Biophys Res Commun 2008 (Breast Neoplasms) : Here we propose that, rather than inhibiting PTEN function, CKIepsilon positively regulates Akt possibly by inhibiting Protein Phosphatase 2A (PP2A)
Jun et al., Obesity (Silver Spring) 2008 (Disease Models, Animal...) : These data suggest that HFD might have a relevance to insulin resistance by increasing the expression of PP2A , an inhibitor of AKT activity in the phosphatidylinositol 3-kinase (PI3K)/AKT pathway, and also by suppressing the expression of TC10 and CIP4, downstream effectors of the Cbl/CAP/TC10 insulin signaling cascade in the visceral adipose tissue
Hong et al., J Biol Chem 2008 : A novel Epac-Rap-PP2A signaling module controls cAMP dependent Akt regulation ... Here we show that ( i ) upstream regulators, PIK and PDK1, are not the target ( s ) of the cAMP inhibitory action ; ( ii ) constitutively active Akt and calyculin A-stimulated Akt are resistant to cAMP inhibition, suggesting the action of a phosphatase ; ( iii ) cAMP increases the rate of Akt dephosphorylation, directly implicating an Akt-phosphatase ; ( iv ) Epac- and protein kinase A (PKA)-specific analogs synergistically inhibit Akt, indicating the involvement of both cAMP dependent effector pathways ; ( v ) H89 and dominant negative Epac 279E block cAMP-inhibitory action ; ( vi ) Epac associates in a complex with Akt and PP2A, and the associated-phosphatase activity is positively modulated by cAMP in a PKA- and Rap1 dependent manner ; ( vii ) like its action on Akt inhibition, PKA- and Epac-specific analogs synergistically activate Epac associated PP2A ; and ( viii ) dominant negative PP2A blocks cAMP-inhibitory action
Chan et al., Cell Biol Int 2009 : Collectively, these findings suggest that PP2A and PTEN may be involved in fine tuning the regulation of Akt/tuberin/mTOR/p70S6K in PC12 cells by M ( 4 ) mAChR and TrkA, respectively
Cao et al., Free Radic Biol Med 2009 (Leukemia) : Further experiments indicate that the conformational change in Akt not only disrupts Akt-Hsp90 binding, but also enhances Akt-PP2A interaction
Switzer et al., Oncogene 2009 (Breast Neoplasms...) : Dithiolethione compounds inhibit Akt signaling in human breast and lung cancer cells by increasing PP2A activity
O'Shaughnessy et al., Development 2009 : Akt dependent Pp2a activity is required for epidermal barrier formation during late embryonic development ... We therefore describe a novel Akt dependent Pp2a activity that acts at least partly through Jun to affect initial barrier formation during late embryonic epidermal development
Werden et al., J Virol 2010 (Neoplasms) : In contrast, the PP2A-specific phosphatase inhibitor okadaic acid promoted increased Akt kinase activation and rescued MYXV replication in human cancer cells that did not previously support viral replication
Switzer et al., Oncogene 2011 (Neoplasms) : COG112 mediated increases in PP2A activity resulted in the inhibition of Akt signaling and cellular proliferation
Galbo et al., PloS one 2011 (Insulin Resistance) : Furthermore, inhibition of PP2A by specific inhibitors increased insulin stimulated activation of Akt and phosphorylation of FoxO1 and Gsk3a
Chang et al., PloS one 2012 (Colonic Neoplasms) : Our results indicate that epirubicin decreased the intracellular ROS in GRP78 knockdown cells, which decreased survival signaling through both the Akt pathway and the activation of PP2A
Zhang et al., Diabetes 2012 (Hypertension...) : We conclude that ceramide mediates obesity related vascular dysfunction by a mechanism that involves PP2A mediated disruption of the eNOS/Akt/Hsp90 signaling complex
Chen et al., Bioorg Med Chem 2012 : Several studies have shown that downregulation of CIP2A by small molecules reduces PP2A dependent phosphorylation of Akt and induces cell death
Li et al., J Biol Chem 2013 : Collectively these results suggest that rapamycin induces PP2A dependent and DNA-PK mediated Akt phosphorylation
Leonard et al., Cell cycle (Georgetown, Tex.) 2013 : Inhibition of Akt activation with MK2206 reduced the whole-cell and centrosome levels of PLK-1 and ?-tubulin and also prevented the recruitment of PTEN to mitotic centrosomes
Kobayashi et al., Br J Pharmacol 2013 : The inhibition of Akt phosphorylation by SOL was due to increased PP2A phosphatase activity, which was reduced in COPD and oxidative stress model