PEBP1 (phosphatidylethanolamine binding protein 1) serves as a critical regulatory scaffold protein that controls ferroptosis, a form of iron-dependent programmed cell death driven by lipid peroxidation. The primary function of PEBP1 involves forming complexes with 15-lipoxygenase enzymes (15LO1 and 15LO2), fundamentally altering their substrate specificity to enable the oxygenation of polyunsaturated phosphatidylethanolamines rather than free fatty acids 1. This PEBP1-15LO interaction is essential for generating lipid death signals that execute ferroptosis when antioxidant systems like GPX4 become insufficient 1. PEBP1's mechanism involves facilitating 15-lipoxygenase localization to plasma membrane phospholipids through corticosteroid-activated PKC pathways, particularly during stress conditions 2. The protein demonstrates significant disease relevance across multiple pathological contexts, including asthma airway epithelial cells, kidney epithelial cells in renal failure, and cortical/hippocampal neurons in brain trauma 1. In Parkinson's disease, PEBP1 promotes dopaminergic neuron loss through membrane phospholipid peroxidation, with stress-induced corticosteroids enhancing this process 2. Additionally, PEBP1 functions as an autophagy modulator that can determine ferroptotic responses in a context-dependent manner 3. Clinically, PEBP1 has emerged as a biomarker in various cancers and represents a promising therapeutic target for drug discovery aimed at modulating ferroptotic cell death 1.