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AKT1 — CDC42

Text-mined interactions from Literome

Genot et al., Mol Cell Biol 2000 : We show that in Jurkat cells, activated forms of Rac1 or Cdc42 , but not Rho, stimulate an increase in Akt/PKB activity ... We show that in Jurkat cells, activated forms of Rac1 or Cdc42 , but not Rho, stimulate an increase in Akt/PKB activity
Gakidis et al., J Cell Biol 2004 : beta2 induced activation of Cdc42 , Rac1, and RhoA is defective in Vav1/3ko neutrophils, and phosphorylation of Pyk2, paxillin, and Akt is also significantly reduced
Lee et al., Histochem Cell Biol 2006 : In this report, we describe that S1P stimulated cortactin translocation to the cell periphery to form lamellipodia is specifically mediated by the endothelial S1P1 G-protein coupled receptor, and is regulated by G ( i ) -mediated Akt dependent S1P1 receptor phosphorylation and Cdc42/Rac activation pathways
Reville et al., J Immunol 2006 : Polarized distribution of Cdc42 is associated with Akt/PKB mediated Cdc42 activation
Morley et al., Cell Signal 2007 (Cell Transformation, Neoplastic) : We found that Dbl induced the phosphorylation of Akt on threonine 308, through the GTPases Rac and Cdc42 and in a PI3-kinase dependent manner
Jin et al., Neurochem Int 2007 : These results suggest that the NGF induced ruffling requires activation of Rac1 and Cdc42 , but does not require Ras, PI-3k, Akt and GSK-3beta
Carlin et al., Science signaling 2011 (Neoplasms) : In addition, the kinase Akt and the p85a subunit of phosphoinositide 3-kinase (PI3K) were required for Cdc42 activation, the periodicity of the oscillation in Cdc42 activity, and the subsequent polarization of cytotoxic vesicles toward target cells
Stengel et al., PloS one 2012 (Cell Transformation, Neoplastic) : The loss of Cdc42 in Ras transformed cells results in reduced Akt signaling, restoration of which could partially rescues the proliferation defects associated with Cdc42 loss
Clark et al., J Cell Biol 1998 : Furthermore, we observed that Cdc42 controls the integrin dependent activation of extracellular signal regulated kinase 2 and of Akt , a kinase whose activity has been demonstrated to be dependent on phosphatidylinositol (PI) 3-kinase