DnaJ heat shock protein family (Hsp40) member C11 (DNAJC11)

DnaJ heat shock protein family (Hsp40) member C11 (DNAJC11) is a mitochondrial protein and member of the J protein (Hsp40) co-chaperone family, defined by a conserved N-terminal J domain. DNAJC11 participates in the organization of the mitochondrial inner membrane, specifically in cristae formation, via physical association with the MICOS and SAM complexes at the mitochondrial membrane. As a co-chaperone, it is presumed to regulate Hsp70-mediated ATP hydrolysis and assist with protein folding, complex assembly, and protein translocation across membranes. DNAJC11 is expressed in multiple tissues and localizes to distinct submitochondrial compartments, with its major isoform found both peripherally on the outer membrane and within internal mitochondrial structures. Mutations in DNAJC11 can disrupt mitochondrial architecture, leading to neuromuscular phenotypes and motor neuron pathology in animal models. No direct disease therapies, drugs, or established biomarker roles are currently associated with DNAJC11.

Other names

DnaJ homolog subfamily C member 11FLJ10737dJ126A5.1novel DnaJ domain-containing proteinDJC11