PLAAT1 (phospholipase A and acyltransferase 1) is a dual-function enzyme that exhibits both phospholipase A1/2 and acyltransferase activities, playing crucial roles in phospholipid metabolism and organelle homeostasis 1. The enzyme catalyzes calcium-independent release of fatty acids from glycerophospholipids and transfers fatty acyl groups to form N-acylphosphatidylethanolamine (NAPE), serving as a precursor for bioactive N-acylethanolamines (NAEs) 1. PLAAT1 localizes primarily to the endoplasmic reticulum with some mitochondria-associated presence and functions as a novel phosphatidylcholine:monolysocardiolipin transacylase, contributing to cardiolipin remodeling 2. Mechanistically, PLAAT1 overexpression triggers mitochondrial fragmentation and peroxisome reduction in an enzyme activity-dependent manner, altering the expression of key mitochondrial dynamics proteins including dynamin-related protein 1, optic atrophy 1, and mitofusin 2 3. The protein is essential for organelle degradation during lens fiber cell maturation, with deficiency causing cataract formation in animal models 14. Clinically, PLAAT1 has been identified as a component of prognostic models for lung squamous cell carcinoma, suggesting potential therapeutic relevance 5.