Phosphorylation of Akt at S473 in the carboxy-terminal hydrophobic motif, either by mTOR () or by DNA-PK (), stimulates full Akt activity. Full activation of Akt leads to additional substrate-specific phosphorylation events in both the cytoplasm and nucleus, including inhibitory phosphorylation of the pro-apoptotic FOXO proteins ().

Fully active PKB/Akt mediates numerous cellular functions including angiogenesis, metabolism, growth, proliferation, survival, protein synthesis, transcription, and apoptosis (as shown in ). Dephosphorylation of T308 by PP2A (), and S473 by PHLPP1/2 (), and the conversion of PIP 3 to PIP 2 by PTEN () antagonize Akt signaling.

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