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Physicochemical compatibility

Phosphorylation of S473 in the PIF motif of RAC-alpha serine/threonine-protein kinase (AKT1) by Serine/threonine-protein kinase mTOR (MTOR) (as part of mTORC2 complex) induces intramolecular interaction with the PIF-binding pocket, resulting in cis-activation of RAC-alpha serine/threonine-protein kinase (AKT1). Dephosphorylation of the PIF motif by PHLPP1/2 (PHLPP1 for Akt2/3 and PHLPP2 for Akt1/3) results in reduced Akt activity, probably by disrupting the interaction with the Akt PIF pocket and thus cis-activation.

(1) RAC-alpha serine/threonine-protein kinase (AKT1)


(1) Common polymorphism in the phosphatase PHLPP2 results in reduced regulation of Akt and protein kinase C.
Brognard et al. J. Biol. Chem. (2009)

See also

Other switches involving participants
RAC-alpha serine/threonine-protein kinase (AKT1) - 2 more (view)

Other switches involving interfaces
DOC_AGCK_PIF_1 - 9 more (view)
Protein kinase domain - 35 more (view)

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