mTORC2 phosphorylates AKT1 on serine-473

Stable Identifier
R-HSA-9860800
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Suppression of the RICTOR subunit of the mTORC2 complex blocks flow-induced phosphorylation of serine-473 of AKT1 (Jin et al. 2021). The mTORC2 complex has been shown to directly phosphorylate AKT1 (Sarbassov et al. 2005). mTORC2 is likely activated by PI3K signaling as PI3K activity is required for phosphorylation of serine-473 of AKT1 in response to shear flow stress (Jin et al. 2021). 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
15718470 Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, DD, Guertin, DA, Ali, SM, Sabatini, DM

Science 2005
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
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Catalyst Activity

protein serine/threonine kinase activity of TORC2 complex [cytosol]

This event is regulated
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