PDK1 (3-phosphoinositide-dependent protein kinase) is activated by the presence of PtdIns (3, 4, 5) P3 or PtdIns (3, 4) P2. PDK1 then activates protein kinase B (PKB) which, in turn, inactivates glycogen synthase kinase-3 (GSK3). The phosphorylation of other proteins by PKB and GSK3 is likely to mediate many of the intracellular actions of insulin. Thus, PDK1 plays a key role in mediating many of the actions of the second messenger(s) PtdIns (3, 4, 5) P3 and/or PtdIns (3, 4) P2. The human PDK1 is a 556-residue monomeric enzyme comprising of a catalytic domain that is most similar to the PKA, PKB and PKC subfamily of protein kinases.

PDPK1 (3-phosphoinositide dependent protein kinase 1) is a serine/threonine protein kinase which is activated upon accumulation of PIP3 (phosphatidylinositol-3,4,5-trisphosphate), a PI3K (phosphoinositide 3-kinase) product. It controls AGC (protein kinase A, G, and C) kinase members, such as AKT (v-akt murine thymoma viral oncogene homolog), p70 ribosomal S6 kinase (S6K), serum- and glucocorticoid-induced protein kinase (SGK), and protein kinase C (PKC) members. It is involved in metabolism, growth, proliferation, and survival. PDPK1 is associated with growth of angiosarcoma cells.

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