Inositol polyphosphate multikinase (IPMK)

Inositol polyphosphate multikinase (IPMK) is a multifunctional enzyme in the inositol phosphate kinase (IPK) superfamily that plays a central role in cellular signal transduction. Its primary catalytic activities are phosphorylation of soluble inositol phosphates (e.g., converting inositol 1,4,5-trisphosphate to inositol 1,3,4,5,6-pentakisphosphate) and lipid kinase activity converting phosphatidylinositol 4,5-bisphosphate (PIP2) to phosphatidylinositol 3,4,5-trisphosphate (PIP3), which is a critical step in activating the PI3K/AKT/mTOR pathway. In addition to its enzymatic functions, IPMK acts as a non-catalytic regulator of protein complexes and transcriptional coactivator for major regulators such as p53, serum response factor, and CBP/p300, influencing gene expression, cell growth, metabolic state, and apoptosis. Given its diverse roles, IPMK is implicated in cancer, neurological, and metabolic diseases and represents an emerging therapeutic target, though direct pharmacological targeting remains experimental.

Other names

Inositol polyphosphate multikinaseIPMKIMPKInositol 1,3,4,6-tetrakisphosphate 5-kinaseinositol 1,3,4,6-tetrakisphosphate 5-kinase

Potential small-molecule kinase inhibition (by antagonizing either inositol phosphate kinase or PI3K activity). Modulation of protein-protein interactions in non-catalytic regulatory roles.