PLAA (phospholipase A2 activating protein) is a multifunctional ubiquitin-binding protein that regulates protein trafficking and degradation. As a key component of the VCP/p97 interactome, PLAA mediates ubiquitin-dependent sorting of membrane proteins to late endosomes via ESCRT-dependent mechanisms and promotes synaptic vesicle recycling 1. Beyond protein degradation pathways, PLAA regulates P-body assembly through its intrinsically disordered region, enabling mRNA processing and decapping complex recruitment 2. PLAA positively regulates cytosolic phospholipase A2 activity in response to TNF-Ξ± and lipopolysaccharide, controlling prostaglandin E2 biosynthesis 3. The protein also participates in lysophagy, facilitating clearance of damaged lysosomes during lysosomal membrane permeabilization 4. Clinically, PLAA mutations cause neurodevelopmental disorders with progressive microcephaly, spasticity, and brain anomalies 1. De novo missense variants in the PUL domain impair PLAA-p97/VCP interaction, leading to abnormal vesicle recycling and neurological phenotypes including intellectual disability, autism spectrum disorders, and psychomotor regression 15. Additionally, PLAA downregulation in ovarian cancer associates with enhanced metastasis through dysregulation of the METTL3-TRPC3 axis 6, highlighting PLAA's emerging role in cancer progression.