Multiple inositol polyphosphate phosphatase 1 (MINPP1)

Multiple inositol polyphosphate phosphatase 1 (MINPP1) is a member of the histidine acid phosphatase superfamily, primarily localized to the endoplasmic reticulum, where it hydrolyzes higher inositol polyphosphates such as inositol hexakisphosphate (InsP6) and inositol pentakisphosphate (Ins(1,3,4,5,6)P5) to lower phosphorylated species[2][3][4][5]. MINPP1 plays a crucial role in regulating diverse cellular processes, including calcium signaling, apoptosis, bone and cartilage formation, ER stress response, and iron metabolism[2][3][4][5]. Loss-of-function mutations in MINPP1 are causative for pontocerebellar hypoplasia, a severe neurodevelopmental disorder[2][3]. Emerging evidence suggests tissue- and context-dependent subcellular localizations and multiple isoforms, with possible secreted forms influencing the tumor microenvironment[1][3]. No targeted drugs against MINPP1 are currently established in clinical use.

Other names

MINPP1Minpp1Multiple inositol polyphosphate phosphataseMIPPMINPP

Dephosphorylation of inositol polyphosphates, modulating intracellular signaling pathways (e.g., reducing levels of InsP6 and Ins(1,3,4,5,6)P5) Potential indirect modulation of inositol lipid pathways (e.g., affecting phosphatidylinositol-3,4,5-trisphosphate signaling when mislocalized)[2].