DNAJA2 is a co-chaperone protein that works with HSC70/HSP70 chaperones to regulate protein folding and quality control. As a member of the HSP40 family, DNAJA2 stimulates ATP hydrolysis and protein folding mediated by HSPA1A/B 1. The protein forms highly-ordered tubular structures that can be dissociated by HSC70, with oligomer dissociation into dimers enhancing its interaction with unfolded client proteins 2. DNAJA2 plays critical roles in cellular homeostasis by maintaining centrosome stability through chaperone-mediated autophagy of centriolar satellite proteins PCM1 and CEP290 3. It also regulates insulin signaling by binding to insulin receptors and preventing spontaneous endocytosis, thereby maintaining glucose homeostasis 4. In protein quality control, DNAJA2 buffers proteasomal degradation of cytosolic proteins with missense mutations, acting to stabilize wild-type proteins while specifically buffering mutant proteins to reduce their turnover 5. The protein can suppress aggregation of disease-associated proteins like TDP-43 by stabilizing extended conformations 6. DNAJA2 deficiency leads to genomic instability and activates immune responses, while also causing neonatal lethality in knockout mice due to disrupted glucose metabolism 34.