1-acyl-sn-glycerol-3-phosphate acyltransferase 3 (AGPAT3) (AGPAT3)

Golgi-associated lysophospholipid acyltransferase, scientifically identified as 1-acyl-sn-glycerol-3-phosphate acyltransferase 3 (AGPAT3 or LPAAT3), is an integral membrane enzyme localized to the Golgi complex and endoplasmic reticulum [10, 14]. It plays a critical role in the Lands cycle by catalyzing the conversion of lysophospholipids, specifically lysophosphatidic acid (LPA), into phospholipids like phosphatidic acid (PA) through the addition of an acyl group [12, 15]. This enzymatic activity is essential for maintaining the specific lipid composition of organelle membranes, which in turn regulates membrane curvature and the formation of transport tubules [1, 11]. By converting cone-shaped lysophospholipids into cylindrical phospholipids, AGPAT3 acts as a negative regulator of membrane tubulation [10, 12]. Inhibition of this enzyme, notably by the compound CI-976 (PD 128042), leads to an accumulation of lysophospholipids that promote excessive Golgi tubulation and retrograde trafficking from the Golgi to the ER [5, 11]. Consequently, it is a key regulator of Golgi structure and protein trafficking, making it a subject of interest in studies of cellular organization and diseases involving secretory pathway dysfunction, such as cancer [2, 14].

Other names

Golgi-associated lysophospholipid acyltransferaseLysophosphatidic acid acyltransferase 3LPAAT3LPAAT-gamma1-AGP acyltransferase 31-acyl-sn-glycerol-3-phosphate O-acyltransferase 3

Lysophospholipid acyltransferase inhibition