◀ Back to AKT1

AKT1 — INPP5D

Text-mined interactions from Literome

Freeburn et al., J Immunol 2002 : Expression of a constitutively active SHIP-1 protein in Jurkat cells was sufficient to reduce both constitutive PKB membrane localization and PKB phosphorylation
Baran et al., J Biol Chem 2003 : The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony stimulating factor induced Akt activity ... Because the inositol 5'-phosphatase SHIP-1 is an important regulator of intracellular levels of phosphatidylinositol 3,4,5-trisphosphate, an important second messenger necessary for Akt activation, we hypothesized that SHIP-1 was involved in the regulation of M-CSF receptor (M-CSF-R) induced Akt activation ... Transfection of 3T3-Fms cells, which express the human M-CSF-R, with wild-type SHIP-1 showed that SHIP-1 was necessary for the negative regulation of M-CSF induced Akt activation ... These data provide the first evidence of the involvement of both SHIP-1 and Lyn in the negative regulation of M-CSF-R induced Akt activation
Tanigaki et al., Circ Res 2009 : Thus, CRP inhibits eNOS stimulation by insulin via FcgammaRIIB and its ITIM, SHIP-1 activation , and resulting blunted activation of Akt
Harris et al., J Immunol 2011 : Silencing of SHIP-1 leads to increased basal phosphorylation of protein kinase B/Akt and its substrate GSK3ß, as well as an increase in basal levels of polymerized actin, suggesting that SHIP-1 might regulate changes in the cytoskeleton ... Silencing of SHIP-1 leads to increased basal phosphorylation of protein kinase B/Akt and its substrate GSK3ß, as well as an increase in basal levels of polymerized actin, suggesting that SHIP-1 might regulate changes in the cytoskeleton
Kumar et al., Cell Microbiol 2012 : Bach1 is a transcriptional repressor of haem oxygenase-1 (HO-1), whereas SHIP1 inhibits the activation of the serine/threonine kinase AKT