DnaJ homolog subfamily B member 6 (DNAJB6)

DnaJ homolog subfamily B member 6 (DNAJB6) is a highly conserved molecular chaperone in the Hsp40 (DNAJ) family, characterized by its J-domain and oligomeric structure[1][3]. It exists as at least two isoforms (DNAJB6a, nuclear; DNAJB6b, cytoplasmic) and acts both in concert with and independently of Hsp70 to prevent toxic protein aggregation, notably amyloid β and polyglutamine fibril formation, which underlie several neurodegenerative diseases[1][2][4]. DNAJB6 is also implicated in tumor suppression, mediating downregulation of oncogenic signaling pathways and facilitating cell-cycle arrest. Mutations in a conserved domain are causative for limb-girdle muscular dystrophy type D1, marked by muscle protein inclusions and myofibrillar disruption. Beyond maintaining proteostasis, DNAJB6 functions in nuclear import of regulatory proteins and virus infection pathways. Its unique S/T-rich region and ability to form dynamic oligomers distinguish its anti-aggregation activity from other chaperones[1][2][3][4].

Other names

DNAJB6MRJDJ4HSJ2MSJ-1MSJ1HHDJ1HSJ-2LGMD1DLGMDD1DnaJ (Hsp40) homologHeat shock protein J2DnaJ-like 2 protein

Molecular chaperoning: prevents the aggregation of misfolded proteins and amyloid formation Facilitates the handover of misfolded proteins to Hsp70 (a major molecular chaperone) Suppression of signaling pathways promoting oncogenesis (e.g., upregulation of DKK1, inhibition of Wnt/β-catenin and AKT) Promoting cell-cycle arrest via nuclear import of regulatory proteins