AKT1 dephosphorylation by PP2A-B56-beta,gamma

Stable Identifier
Homo sapiens
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The protein phosphatase 2A (PP2A) complex containing a regulatory subunit B56 beta (PPP2R5B) or B56 gamma (PPP2R5C) dephosphorylates activated AKT1 on threonine residue T308 and serine residue S473, thus halting PI3K/AKT signaling (Rocher et al. 2007). Phosphatidylinositol-5-phosphate (PI5P) negatively regulates PP2A-mediated dephosphorylation of AKT1 by promoting, through an unknown mechanism, an inhibitory phosphorylation on tyrosine residue Y307 (Chen et al. 1992) of the catalytic subunit of PP2A (Ramel et al. 2009).

Literature References
PubMed ID Title Journal Year
1325671 Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation

Chen, J, Martin, BL, Brautigan, DL

Science 1992
19576174 PtdIns5P protects Akt from dephosphorylation through PP2A inhibition

Leslie, N, Ramel, D, Chicanne, G, Gaits-Iacovoni, F, Lagarrigue, F, Tronchère, H, Payrastre, B, Dupuis-Coronas, S

Biochem. Biophys. Res. Commun. 2009
17200115 Inhibition of B56-containing protein phosphatase 2As by the early response gene IEX-1 leads to control of Akt activity

Rocher, G, Letourneux, C, Porteu, F, Lenormand, P

J. Biol. Chem. 2007
Event Information
Catalyst Activity

protein serine/threonine phosphatase activity of PP2A-B56-beta,gamma [cytosol]

This event is regulated
Negatively by
Orthologous Events
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