DnaJ heat shock protein family member B2 (DNAJB2)

DnaJ heat shock protein family member B2 (DNAJB2) is a molecular chaperone protein in the Hsp40 family, primarily expressed in neurons. DNAJB2 acts as a co-chaperone that binds unfolded and misfolded proteins, facilitating their correct folding and promoting their ubiquitin-dependent degradation via the proteasome, mostly through regulation and activation of Hsp70 chaperones[1][2]. It plays an essential role in neuronal proteostasis, protecting cells from toxic protein aggregation. Two major isoforms—DNAJB2a (cytosolic/nuclear) and DNAJB2b (membrane-associated)—have distinct cellular localizations but share core functions[1]. Disease-linked mutations in *DNAJB2* lead to inherited neurodegenerative diseases, such as Charcot-Marie-Tooth disease type 2T and distal hereditary motor neuropathies, through loss of chaperone-mediated protein quality control[1]. DNAJB2 is being investigated as a potential therapeutic target for reducing toxic protein inclusions in neurodegenerative conditions, although no drugs currently target this chaperone directly[1][2].

Other names

DnaJ homolog subfamily B member 2HSJ1HSPF3HSJ-1CMT2THeat shock 40 kDa protein 3Heat shock protein J1DSMA5HMNR5neuronal DNAJ-like 1dnaJ protein homolog 1

Enhancement of proteasomal degradation of misfolded proteins; Modulation of Hsp70 chaperone function; Inhibition of toxic protein aggregation; Protein homeostasis restoration