DnaJ heat shock protein family (Hsp40) member C24 (DNAJC24)

DnaJ heat shock protein family (Hsp40) member C24 (abbreviated DNAJC24) is an evolutionarily conserved heat shock protein that acts as a co-chaperone, stimulating ATPase activity in Hsp70-type chaperones, and is critical for diphthamide biosynthesis, a post-translational modification in translation elongation factor 2 (EEF2)[1][8]. This modification is the target for inactivation by diphtheria toxin and Pseudomonas exotoxin A. DNAJC24 possesses iron-binding and electron-carrying properties and regulates cellular stress responses including protein folding, autophagy, and cell motility[1][2][8]. DNAJC24 expression is elevated in several cancers (notably hepatocellular carcinoma and lung adenocarcinoma), correlates with poor prognosis, and may serve as a biomarker and potential therapeutic target to inhibit cancer cell proliferation by disrupting cellular stress adaptation and ammonia metabolism[2][5].

Other names

DPH4ZCSL3JJJ3CSL-type zinc finger-containing protein 3Diphthamide biosynthesis protein 41700030A21RikDPH4 homolog (JJJ3, S. cerevisiae)JJJ3 homolog

Targeting DNAJC24 (e.g., by RNA interference) can suppress cell proliferation, motility, and autophagy in HCC cells, interfering with ammonia metabolism and possibly other stress-related pathways