Gene interactions and pathways from curated databases and text-mining

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CDC42 — PIK3CA

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Zeng et al., J Biol Chem 2002 : As expected, CDC42 and Rac1 activation mediated by EGLT can be completely inhibited by PI3K inhibitors, wortmannin and LY294002, and the p85 dominant negative mutant but not by either the phospholipase C inhibitor, or an intracellular Ca ( 2+ ) chilator BAPTA/AM ... As expected, CDC42 and Rac1 activation mediated by EGLT can be completely inhibited by PI3K inhibitors, wortmannin and LY294002, and the p85 dominant negative mutant but not by either the phospholipase C inhibitor, or an intracellular Ca ( 2+ ) chilator BAPTA/AM
Chen et al., J Biol Chem 2004 (Cryptosporidiosis) : The cellular expression of either a dominant negative mutant of PI3K ( PI3K-Deltap85 ) or functionally deficient mutants of frabin inhibited C. parvum induced Cdc42 accumulation at the host cell-parasite interface
Chang et al., J Biomed Sci 2005 : Suppression of PI3K activity in integrin alpha6beta1 activated platelets induces an increase in Cdc42 activity and more filopodium formation
Nizhynska et al., Dev Neurobiol 2007 : Moreover, agrin induced activation of Rac and Cdc42 is impaired in the presence of PI3-K inhibitors
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
Babbin et al., J Immunol 2007 : Taken together, theses results support a novel role for FPR stimulation in enhancing intestinal epithelial cell restitution through PI3K dependent activation of Rac1 and Cdc42
Samaga et al., PLoS Comput Biol 2009 (Liver Neoplasms) : Our results strongly suggest that the Rac/Cdc42 induced p38 and JNK cascades are independent of PI3K in both primary hepatocytes and HepG2
Beemiller et al., Mol Biol Cell 2010 : Inhibition of PI3K resulted in persistently active Cdc42 and Rac1, but not Rac2, in stalled phagocytic cups ... Expression of constitutively active Cdc42 ( G12V ) increased 3'PI concentrations in plasma membranes and small phagosomes, indicating a role for Cdc42 in PI3K activation
Makrodouli et al., Molecular cancer 2011 (Colonic Neoplasms...) : In parallel, KRASG12V enhances the ability of colon adenocarcinoma cells Caco-2 to migrate and invade through filopodia formation and PI3K dependent Cdc42 activation
Keely et al., Nature 1997 (Cell Transformation, Neoplastic...) : PI(3)K inhibition also disrupts actin structures, suggesting that activation of PI(3)K by Cdc42 and Rac1 alters actin organization, leading to increased motility and invasiveness