Suppression of PKN2 eliminates the phosphorylation of AKT1 o...

created [InstanceEdit:9863599] May, Bruce, 2024-03-04
dbId 9863604
displayName Suppression of PKN2 eliminates the phosphorylation of AKT1 o...
literatureReference
modified [InstanceEdit:9906878] May, Bruce, 2024-04-03
schemaClass Summation
text Suppression of PKN2 eliminates the phosphorylation of AKT1 on serine-308, indicating that PKN2 is probably the responsible kinase (Jin et al. 2021). Activity of PI3K, which produces phosphatidylinositol-3,4,5-trisphosphate, is not required for AKT1 phosphorylation on serine-308 (Jin et al. 2021). Phosphorylation of AKT1 on serine-473 by mTORC2 increases phosphorylation of serine-308 by PDPK1 (PDK1) (Sarbassov et al. 2005). AKT1 phosphorylated on serine-308 and serine-473 is located at the plasma membrane at cell-cell junctions in endothelial cells experiencing unidirectional laminar shear stress, but it is perinuclear in cells experiencing disturbed flow (Melchior and Frangos 2014).
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