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CDC42 — PIK3CA
Pathways - manually collected, often from reviews:
-
KEGG Bacterial invasion of epithelial cells:
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
→
CDC42
(protein-protein, activation)
-
NCI Pathway Database CDC42 signaling events:
CDC42/GTP complex (CDC42)
→
PI3K complex (PIK3CA-PIK3R1)
(modification, activates)
Tolias et al., J Biol Chem 1995*, Zheng et al., J Biol Chem 1994*, Keely et al., Nature 1997*
Evidence: assay, physical interaction
-
NCI Pathway Database Nongenotropic Androgen signaling:
RAC1-CDC42/GDP complex (RAC1_CDC42)
→
PI3K complex (PIK3CA-PIK3R1)
(modification, collaborate)
Papakonstanti et al., Mol Endocrinol 2003*
Evidence: assay
-
NCI Pathway Database Osteopontin-mediated events:
Rho Family GTPase-active (RHOA/CDC42/RAC1)
→
PI3K complex (PIK3CA-PIK3R1)
(modification, activates)
Biswas et al., BMC cell biology 2004*, Chellaiah et al., Mol Biol Cell 1996
Evidence: mutant phenotype, assay
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