The esterification of a fatty acyl moiety to diacylglycerol to form triacylglycerol (TAG) is catalysed by two diacylglycerol O-acyltransferases (DGATs) encoded by genes belonging to two distinct gene families. The enzymes are referred to as DGAT1 and DGAT2 in order of their identification. Both proteins are transmembrane proteins localized in the endoplasmic reticulum. Their membrane topologies are however significantly different. This difference is hypothesized to give the two isozymes different abilities to interact with other proteins and organelles and access to different pools of fatty acids, thereby creating a distinction between the enzymes in terms of their role and contribution to lipid metabolism. DGAT1 is proposed to have dual topology contributing to TAG synthesis on both sides of the ER membrane and esterifying only the pre-formed fatty acids. There is evidence to suggest that DGAT2 translocates to the lipid droplet (LD), associates with other proteins, and synthesizes cytosolic and luminal apolipoprotein B associated LD-TAG from both endogenous and exogenous fatty acids. The aim of this review is to differentiate between the two DGAT enzymes by comparing the genes that encode them, their proposed topologies, the proteins they interact with, and their roles in lipid metabolism.
Keywords: Diacylglycerol acyltransferase; Lipid accumulation; Lipid droplet; Lipid metabolism; Liver; Triacylglycerol; Very low density lipoprotein.
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