Reactome | Once AKT is localized at the plasma membrane, it is phosphor...

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created	[InstanceEdit:198362] Jassal, B, 2007-06-11 10:01:50
dbId	198363
displayName	Once AKT is localized at the plasma membrane, it is phosphor...
literatureReference	[LiteratureReference:199373] Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex [LiteratureReference:199317] Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B [LiteratureReference:9755776] SARS-CoV-2 Membrane Glycoprotein M Triggers Apoptosis With the Assistance of Nucleocapsid Protein N in Cells
modified	[InstanceEdit:9766206] Shamovsky, Veronica, 2022-02-18
schemaClass	Summation
text	Once AKT is localized at the plasma membrane, it is phosphorylated at two critical residues for its full activation. These residues are a threonine (T308 in AKT1) in the activation loop within the catalytic domain, and a serine (S473 in AKT1), in a hydrophobic motif (HM) within the carboxy terminal, non-catalytic region. PDPK1 (PDK1) is the activation loop kinase; this kinase can also directly phosphorylate p70S6K. The HM kinase, previously termed PDK2, has been identified as the mammalian TOR (Target Of Rapamycin; Sarbassov et al., 2005) but several other kinases are also able to phosphorylate AKT at S473. Phosphorylation of AKT at S473 by TORC2 complex is a prerequisite for PDPK1-mediated phosphorylation of AKT threonine T308 (Scheid et al. 2002, Sarabassov et al. 2005).

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