Gene interactions and pathways from curated databases and text-mining

◀ Back to AKT1

AKT1 — PIKFYVE

Text-mined interactions from Literome

Berwick et al., J Cell Sci 2004 : Finally, we demonstrate that overexpression of a PIKfyve [ S318A ] mutant in 3T3-L1 adipocytes enhances insulin stimulated IRAP/GLUT4 vesicle translocation to the plasma membrane suggesting a role for PKB dependent phosphorylation of PIKfyve in insulin regulated IRAP/GLUT4 trafficking
Ikonomov et al., Exp Cell Res 2007 : Loss of PIKfyve-ArPIKfyve reduced insulin stimulated Akt phosphorylation and the cell surface accumulation of GLUT4 or IRAP, but not GLUT1 containing vesicles without affecting overall expression of these proteins
Hill et al., Biochem Biophys Res Commun 2010 : We have previously demonstrated that PIKfyve is phosphorylated in response to insulin in a PI3-kinase and protein kinase B (PKB) dependent manner
Munoz et al., J Membr Biol 2013 (Andersen Syndrome) : The ubiquitously expressed protein kinase B ( PKB/Akt ) activates the phosphatidylinositol-3-phosphate-5-kinase PIKfyve , which in turn regulates a variety of carriers and channels
Pakladok et al., Cell Physiol Biochem 2013 : SGK's and PKB/Akt's activate phosphatidylinositol-3-phosphate-5-kinase PIKfyve , which in turn up-regulates several carriers and channels ... SGK's and PKB/Akt's activate phosphatidylinositol-3-phosphate-5-kinase PIKfyve , which in turn up-regulates several carriers and channels ... Conclusion : hERG is up-regulated by PIKfyve , which is in turn activated by PKB/Akt ... Conclusion : hERG is up-regulated by PIKfyve , which is in turn activated by PKB/Akt
Er et al., Science signaling 2013 : Upon EGF stimulation, AKT phosphorylated and activated the kinase PIKfyve [ FYVE containing phosphatidylinositol 3-phosphate 5-kinase ], which promoted vesicle trafficking to lysosomes ... Similar regulation occurred with platelet derived growth factor receptor ( PDGFR ), suggesting that AKT phosphorylation and activation of PIKfyve is likely to be a common feedback mechanism for terminating RTK signaling and reducing receptor abundance