Phospholipase A and acyltransferase 1 (PLAAT1)

Phospholipase A and acyltransferase 1 (PLAAT1) is a human enzyme that belongs to the PLAAT (phospholipase A and acyltransferase) family, characterized by both phospholipase A1/A2 and acyltransferase activities[1][2][3]. PLAAT1 catalyzes the removal of fatty acids from the sn-1 or sn-2 position of glycerophospholipids and facilitates the acylation and transacylation of lysophospholipids and N-acylphosphatidylethanolamines, contributing to phospholipid remodeling, especially in glycerophospholipid and cardiolipin biosynthesis[1][2][3]. PLAAT1 is predominantly localized in the endoplasmic reticulum but also detected in mitochondria-associated membranes[2]. It plays a crucial role in organelle homeostasis, as members of the PLAAT family are necessary for controlled organelle degradation. Disruption or deficiency of PLAAT1 is linked to altered lipid metabolism, resistance to fatty liver disease, and impacts on disorders such as lipodystrophy, cancer, and inflammation[1][3]. No direct drugs or clinical biomarkers are currently established for PLAAT1, but its central roles in lipid metabolism and organelle dynamics suggest it is a potential therapeutic target for metabolic and degenerative diseases[1][2][3].

Other names

HRASLSHRASLS1HRSL1H-REV107A-C1PLA/AT1PLAAT-1HSD28RLP-2Harvey-Ras-like tumor suppressorlecithin:retinol acyltransferase (LRAT)-like protein

Inhibition or modulation of phospholipase A/acyltransferase activity, modulation of cardiolipin remodeling, alteration of N-acylphosphatidylethanolamine formation