DNAJC24 is a type III J-domain heat shock protein (Hsp40 family member) that functions as a cochaperone of Hsp70-type chaperones, stimulating their ATPase activity 1. The protein exhibits iron-binding capability through cysteine residues in its CSL-domain, enabling redox-active and electron-carrier functions critical for diphthamide biosynthesis—a post-translational modification of elongation factor 2 (EEF2) that is targeted by diphtheria toxin and Pseudomonas exotoxin A 1. Iron binding enhances DNAJC24's cochaperone activity and promotes oligomerization, potentially facilitating intracellular iron homeostasis 1. DNAJC24 shows significant disease relevance in multiple malignancies. Elevated expression in hepatocellular carcinoma correlates with shortened patient survival and promotes HCC cell proliferation and motility by modulating ammonia metabolism and autophagy 2. In lung adenocarcinoma, DNAJC24 upregulation predicts poor survival and promotes malignant progression by direct interaction with PCNA and activation of the PI3K/AKT signaling pathway 3. Genetic studies reveal suggestive associations between rare variants of DNAJC24 and late-onset Parkinson's disease 4. Additionally, knockdown of DNAJC24 impairs glucose-stimulated insulin secretion in pancreatic β-cells, suggesting involvement in diabetes pathogenesis in patients with aniridia 5.