Protein O-mannosyltransferase (POMT (also commonly POMT1, POMT2 for human isoforms))

Protein O-mannosyltransferase is a membrane-bound glycosyltransferase enzyme complex located in the endoplasmic reticulum. It is responsible for the transfer of mannose from a dolichol-phosphate-mannose donor to serine/threonine residues of selected proteins, initiating O-mannosylation. This modification is essential for the normal function of α-dystroglycan, and thus for skeletal muscle stability, neuronal migration during brain development, and cell-matrix interactions. In humans, the protein O-mannosyltransferase complex consists of at least two subunits, encoded by POMT1 and POMT2, and defects in these genes cause several forms of congenital muscular dystrophy. In fungi, O-mannosyltransferases are also crucial for pathogenicity and virulence. There are currently no clinically approved drugs targeting human POMTs directly, but genetic defects are the focus of molecular diagnostics and research into therapeutic avenues[1][2][3][4][6].

Other names

MannosyltransferaseProtein O-mannosyltransferase (Pmt in fungi)Dolichyl-phosphate-mannose–protein mannosyltransferase 1 (DPM1)Dolichyl-phosphate-mannose–protein mannosyltransferaseProtein-O-mannosyltransferase 1POMT1_HUMAN (for the human gene/protein)POMT2

Not applicable; therapeutic targeting is mostly conceptual, focusing on potential enzyme replacement or modulation if drugs are developed. Current intervention is primarily genetic or supportive[4].