DnaJ homolog subfamily C member 7 (DNAJC7)

DnaJ homolog subfamily C member 7 (DNAJC7) is a co-chaperone protein in the Hsp40 (DNAJ) family, containing three tetratricopeptide repeat (TPR) domains and a C-terminal J domain. It is primarily expressed in neuronal tissue and plays an essential role in protein homeostasis, especially by regulating the folding, stabilization, and degradation of client proteins in cooperation with molecular chaperones Hsp70 and Hsp90. DNAJC7 acts as a bridge, facilitating transfer of substrate proteins between Hsp70 and Hsp90, and is critically involved in the suppression of pathogenic tau protein aggregation—a hallmark of Alzheimer’s disease and other tauopathies. Mutations in DNAJC7 have been linked to familial forms of amyotrophic lateral sclerosis (ALS) and can exacerbate protein aggregation and neuronal toxicity by disrupting chaperone-mediated quality control. As such, DNAJC7 is considered a potential therapeutic target for the treatment of protein aggregation disorders associated with neurodegenerative diseases

Other names

TPR2TTC2TPR repeat protein 2DJ11DJC7tetratricopeptide repeat domain 2DnaJ heat shock protein family member C7DnaJ (Hsp40) homolog, subfamily C, member 7

Modulation/enhancement of protein quality control via chaperone interaction; Inhibition or facilitation of protein aggregation (notably tau aggregation); Regulation of cellular stress response through interaction with Hsp70/Hsp90 and HSF1-mediated pathways