Cysteine and histidine rich domain containing 1 (CHORDC1)

Cysteine and histidine rich domain containing 1 (CHORDC1) is a zinc-binding co-chaperone protein that interacts with the molecular chaperone Hsp90 and possibly other partners, regulating key processes such as centrosome duplication, chaperone-mediated protein folding, Rho-dependent kinase activity, and particularly the maturation and trafficking of the epidermal growth factor receptor (EGFR). CHORDC1 ensures correct EGFR localization to the plasma membrane, thereby affecting downstream MAPK signaling, cell proliferation, and cytoskeletal organization. Its role is essential for cellular viability, and dysregulation contributes to impaired EGFR signaling, cytoskeletal abnormalities, and can modulate cancer susceptibility and progression. Drugs affecting chaperone activities, like geldanamycin, further highlight the therapeutic relevance of CHORDC1 in cancer and cell biology. CHORDC1 is broadly expressed across human tissues and has several conserved homologs and aliases.

Other names

CHORDC1CHP1CHP-1CHORD domain-containing protein 1Protein morganaMorganaCysteine and histidine-rich domain-containing protein 1CHORD-containing protein 1

Geldanamycin: Hsp90 inhibition decreases EGFR stability, especially in CHORDC1-deficient cells. Potential modulation of chaperone-mediated signaling pathways.