Gene interactions and pathways from curated databases and text-mining

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AKT1 — RAC2

Text-mined interactions from Literome

Yang et al., Immunity 2000 : Rac2 stimulates Akt activation affecting BAD/Bcl-XL expression while mediating survival and actin function in primary mast cells
Genot et al., Mol Cell Biol 2000 : Similar to TCR stimulation, L61Rac induced Akt/PKB kinase activity is also LY294002 and wortmannin sensitive ... Similar to TCR stimulation, L61Rac induced Akt/PKB kinase activity is also LY294002 and wortmannin sensitive
Djouder et al., J Immunol 2001 (Calcium Signaling) : Rac and phosphatidylinositol 3-kinase regulate the protein kinase B in Fc epsilon RI signaling in RBL 2H3 mast cells ... Our results indicate that in rat basophilic leukemia cells Rac and PI3-kinase regulate PKB and suggest that Rac is functionally located upstream and/or parallel of PI3-kinase/PKB in FcepsilonRI signaling
Sánchez-Martín et al., J Biol Chem 2004 : We have identified Vav, a guanine nucleotide exchange factor for Rac-1, and PI3K/Akt, as regulators of the activation and inactivation phases of the activity of Rac-1, respectively, in the context of LFA-1 signaling based on the following experimental evidence : ( i ) LFA-1 induced activation of Vav and PI3K/Akt with kinetics consistent with a regulatory role for these molecules on Rac-1, ( ii ) overexpression of a constitutively active Vav mutant induces activation of Rac independently of LFA-1 stimulation whereas overexpression of a dominant negative Vav mutant blocks LFA-1 mediated Rac activation, ( iii ) pharmacological inhibition of PI3K/Akt prevented the fall in the activity of Rac-1 after its initial activation but had no effect on Vav activity, and ( iv ) overexpression of a dominant negative or a constitutively active Akt-1 induced or inhibited, respectively, Rac-1 activity
Fukuyama et al., Biochem Biophys Res Commun 2004 : Dominant negative Rac severely inhibited PDGF induced osteoblast migration and reduced Akt phosphorylation
Goparaju et al., Mol Cell Biol 2005 : Although S1P(2) deletion had no significant effect on tyrosine phosphorylation of the PDGF receptors or activation of extracellular signal regulated kinase 1/2 or Akt induced by PDGF, it reduced sustained PDGF dependent p38 phosphorylation and markedly enhanced Rac activation
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
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
Zhou et al., J Biol Chem 2006 : Opposing roles for Akt1 and Akt2 in Rac/Pak signaling and cell migration
JeBailey et al., Diabetes 2007 (Insulin Resistance) : Small interfering RNA dependent Rac1 knockdown prevented actin remodeling and GLUT4 translocation but spared Akt phosphorylation, suggesting that Rac and actin remodeling do not contribute to overall Akt activation
Chaigne-Delalande et al., Oncogene 2008 : Constitutively active Rac stimulates Akt activity in T lymphocytes cultured in suspension ... We now show that V12Rac mediated stimulation of Akt is not restricted to the hematopoietic lineage but is dependent on the adherence status of the cell ... V12Rac mediated stimulation of Akt as well as molecular association between Rac and Akt occurred exclusively in cells kept in suspension
Miranti et al., Curr Biol 1998 : This pathway may regulate multiple downstream events in hematopoietic cells, including Rac induced lamellipodia formation, tyrosine phosphorylation of Cbl, and activation of JNK, ERK2 and the phosphatidylinositol 3'-kinase regulated kinase Akt
Nishida et al., Oncogene 1999 : Furthermore, the serine/threonine kinase Akt was stimulated by activated Rac and fetal bovine serum in a synergistic manner