Reactome | p-T816-PKN2 phosphorylates AKT1 on serine-308

p-T816-PKN2 phosphorylates AKT1 on serine-308

Stable Identifier

R-HSA-9860759

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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p-T816-PKN2 phosphorylates AKT1 on serine-308

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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).

Literature References

PubMed ID	Title	Journal	Year
23913776	Distinctive subcellular Akt-1 responses to shear stress in endothelial cells Melchior, B, Frangos, JA	J Cell Biochem	2014
34499618	Protein kinase N2 mediates flow-induced endothelial NOS activation and vascular tone regulation Jin, YJ, Chennupati, R, Li, R, Liang, G, Wang, S, Iring, A, Graumann, J, Wettschureck, N, Offermanns, S	J Clin Invest	2021