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Fig. 8 | Cell Communication and Signaling

Fig. 8

From: Phosphorylation of PP2Ac by PKC is a key regulatory step in the PP2A-switch-dependent AKT dephosphorylation that leads to apoptosis

Fig. 8

Schematic representation of the PKC-induced PP2Ac phosphorylation in the induction of the PP2A switch. In resting cells (first panel), the PP2Ac-IGBP1 dimer binds PI3K, dephosphorylating its inhibitory phosphorylation site (Ser608-p85-PI3K), leading to its activation and consequently cell survival. Upon GqPCR stimulation, PKC phosphorylates PP2Ac on Ser24 residue (second panel). This leads to the release of the IGBP1-PP2Ac dimer form PI3K (third panel), leading to autophosphorylation of PI3K, its inactivation and the detachment of AKT from the plasma membrane. The free PP2Ac-IGBP1 dimer together with PP2Aa bind to the cytoplasmic AKT leading to AKT dephosphorylation, inactivation and consequently cell death (Fourth panel)

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Cell Communication and Signaling

ISSN: 1478-811X