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ARHGEF7 — PIK3CA

Text-mined interactions from Literome

Kusch et al., J Biol Chem 2000 : The regulatory subunit p85 of PI3-K co-immunoprecipitates with Tyk2 but not with Jak1, Jak2, or Jak3, and uPA stimulation increases the PI3-K activity in Tyk2 immunoprecipitates
Bertagnolo et al., Cell Signal 2004 : The Vav/p85 interaction is essential for the ATRA induced PI 3-K activity and for association of PI 3-K with actin, particularly in the nucleus
Wang et al., Biochem J 2007 : In the present study we have demonstrated that : ( i ) PAR-2 increases p110alpha- and p110beta associated lipid kinase activities, and both p110alpha and p110beta are inhibited by over-expression of either beta-arrestin-1 or -2 ; ( ii ) both beta-arrestin-1 and -2 directly inhibit the p110alpha catalytic subunit in vitro, whereas only beta-arrestin-2 directly inhibited p110beta ; ( iii ) examination of upstream pathways revealed that PAR-2 induced PI3K activity required the small GTPase Cdc ( cell-division cycle)42, but not tyrosine phosphorylation of p85 ; and ( iv ) beta-arrestins inhibit PAR-2 induced Cdc42 activation
Berna et al., Cell Signal 2009 (Pancreatic Neoplasms) : These effects are mediated by p85 phosphorylation and activation of PI3K
Aoki et al., Am J Physiol Endocrinol Metab 2009 : PI3K activity associated with IRS-1/2 was not affected by the lack of p85alpha in the liver
Hale et al., Proc Natl Acad Sci U S A 2010 : Overall, these data suggest that both direct binding of NS1 to p85beta ( resulting in repositioning of the N-terminal SH2 domain ) and possible NS1 : p110 contacts contribute to PI3K activation
Maeno et al., J Biol Chem 2012 (Metabolic Diseases) : Thus, PKC and angiotensin induced phosphorylation of Thr-86 of p85/PI3K may partially inhibit the activation of PI3K/eNOS by multiple cytokines and contribute to endothelial dysfunction in metabolic disorders
Comb et al., Mol Cell 2012 (Starvation) : Cells expressing p85 S690A or inhibited for IKK activity exhibit increased Akt activity following cell starvation, demonstrating that p85 phosphorylation is required for starvation induced PI3K feedback inhibition
Furuya et al., J Biol Chem 2013 : The inhibition of p85a expression by siRNA or the inhibition of PI3K by LY294002 prevents the expression of Pdx1, Ngn3, and MafA and the reprogramming to insulin producing cells
Yu et al., Mol Cell Biol 1998 : Importantly, when we examined the effect of p85 on GST-p110alpha in mammalian cells at 30 degrees C, culture conditions that stabilize the catalytic subunit and that are similar to the conditions used for insect cells, we found that p85 inhibited p110alpha ... Thus, we have experimentally distinguished two effects of p85 on p110alpha : conformational stabilization of the catalytic subunit and inhibition of its lipid kinase activity