PLAAT3 (phospholipase A and acyltransferase 3) is a phospholipid-modifying enzyme predominantly expressed in neural and white adipose tissue that functions through dual enzymatic mechanisms. As a phospholipase A1/A2 and acyltransferase, PLAAT3 generates N-acylethanolamines and remodels glycerophospholipids to maintain membrane homeostasis 1. The enzyme plays critical roles in organelle degradation during cellular differentiation; PLAAT3-deficient mice develop cataracts due to impaired organelle clearance in lens fiber cells 2. In viral infection, PLAAT3 acts as a host factor for picornaviruses, facilitating viral genome release and translation through its lipid-modifying activity 3. Clinically, PLAAT3 loss-of-function mutations cause familial partial lipodystrophy type 9, characterized by variable fat loss and metabolic complications including insulin resistance 4. The disease mechanism involves impaired peroxisome proliferator-activated receptor gamma (PPARγ) signaling and defective adipocyte differentiation 4. Beyond lipodystrophy, PLAAT3 upregulation in preeclampsia promotes neutrophil activation via lysophosphatidic acid-LPAR5 signaling 5, and dysregulation associates with colon adenocarcinoma progression 6. As a RAS-responsive tumor suppressor, PLAAT3 downregulation occurs through epigenetic mechanisms in transformed cells 7, suggesting therapeutic potential in metabolic and neoplastic diseases.