FTL (ferritin light chain) is a critical component of the ferritin complex that serves as the primary cellular iron storage protein, maintaining iron in a soluble, non-toxic form essential for iron homeostasis 1. FTL functions by storing iron in the ferrous form and depositing it as ferric hydroxides after oxidation, with iron release mediated through ferritinophagy—a selective autophagy process where NCOA4 delivers ferritin to lysosomes for degradation 2. The protein plays a crucial role in regulating ferroptosis, an iron-dependent form of cell death characterized by lipid peroxidation. Reduced FTL expression sensitizes cells to ferroptosis by decreasing iron storage capacity, as demonstrated in psoriasis where decreased FTL levels correlate with increased ferroptotic cell death 3. In pathological conditions, FTL deficiency has significant consequences—in preeclampsia, reduced FTL triggers ferroptosis in trophoblasts, leading to defective uterine spiral artery remodeling 4. Conversely, FTL upregulation can promote cancer progression by enhancing ferroptosis resistance, as seen in colorectal cancer where AMER1 deficiency increases FTL levels and promotes metastasis 5. Clinically, FTL dysregulation is associated with hyperferritinemia, L-ferritin deficiency, and neurodegeneration with brain iron accumulation, highlighting its importance in iron-related disorders.