The AGPAT2 enzyme catalyzes the acylation of the lysophosphatidic acid at the sn-2 position to form phosphatidic acid, a key intermediate in the biosynthesis of triacylglycerol and glycerophospholipids. High expression of AGPAT2 mRNA in adipose tissue compared with other isoforms suggests that the mutations might affect the adipose tissue the most. Although the precise mechanisms by which AGPAT2 mutations cause lipodystrophy remain unclear, the lack of triglyceride synthesis in the adipocytes or reduced bioavailability of phosphatidic acid and glycerophospholipids such as, phosphatidylinositol, phosphatidylcholine, and phosphatidylethanolamine, which are essential components of cell membranes and play an important in intracellular signaling, could be responsible.