Phosphatidylinositol-glycan biosynthesis class M protein (PIGM)

Phosphatidylinositol-glycan biosynthesis class M protein (PIGM) is a catalytic subunit of the glycosylphosphatidylinositol-mannosyltransferase I complex (GPI-MT-I) located in the endoplasmic reticulum. It catalyzes the transfer of the first alpha-1,4-mannose to glucosaminyl-acyl-phosphatidylinositol (GlcN-acyl-PI), an essential step in the biosynthesis of GPI anchors, which covalently link many proteins to the cell membrane. The GPI anchor is vital for the surface expression and function of numerous GPI-anchored proteins that participate in enzymatic activity, cell adhesion, immune responses, and signaling. Mutations in PIGM disrupt biosynthesis and surface expression of GPI-anchored proteins, resulting in inherited syndromes characterized by neurological symptoms, thrombosis, and other systemic effects. PIGM is widely expressed in human tissues, and its activity is essential for maintaining normal cellular physiology. Currently, there are no approved therapies directly targeting PIGM, but it serves as a crucial enzymatic node in post-translational protein modification and membrane biology[1][2][4][6].

Other names

GPI alpha-1,4-mannosyltransferase IGPI-MT-IGPI mannosyltransferase IGPI mannosyltransferase 1DPM:GlcN-(acyl-)PI mannosyltransferasedol-P-Man dependent GPI mannosyltransferasephosphatidylinositol-glycan biosynthesis class M proteinPIG-M

Not applicable; no known drugs act on PIGM directly in clinical setting. Mechanistic actions would involve inhibition or modulation of GPI anchor biosynthesis.