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).
Chen, J, Martin, BL, Brautigan, DL
Leslie, N, Ramel, D, Chicanne, G, Gaits-Iacovoni, F, Lagarrigue, F, Tronchère, H, Payrastre, B, Dupuis-Coronas, S
Rocher, G, Letourneux, C, Porteu, F, Lenormand, P
protein serine/threonine phosphatase activity of PP2A-B56-beta,gamma [cytosol]
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