IPMK is a multifunctional inositol phosphate kinase with broad substrate specificity that generates critical signaling molecules governing diverse cellular processes. It phosphorylates inositol 1,4,5-trisphosphate sequentially to inositol 1,3,4,5-tetrakisphosphate and inositol 1,3,4,5,6-pentakisphosphate, and also phosphorylates the signaling phospholipid PI(4,5)P2 to produce PIP3 1. Beyond inositol phosphate synthesis, IPMK executes multiple nuclear and cytoplasmic functions: it regulates HDAC3 activity and histone H4 acetylation in a kinase-activity-dependent manner 2, modulates DNA methylation through HDAC1/3-mediated effects on DNMT1 3, and coordinates transcriptional and epigenetic regulation. IPMK plays an essential role in necroptosis by facilitating MLKL oligomerization and membrane localization through inositol pentakisphosphate and inositol hexakisphosphate binding, and is required for normal embryonic development. Recent evidence links IPMK to pathogenic Th2 cell differentiation in asthma, where HIF2α upregulates IPMK to promote TCR-PI3K-AKT signaling and airway inflammation 4. In macrophages, LPS-triggered miR-181c-mediated IPMK downregulation suppresses TLR4-TRAF6 signaling and proinflammatory responses 5. IPMK inhibitors show promise as anticancer agents, with selective effects on inositol phosphate metabolism and transcriptome reprogramming in glioblastoma cells 6.