DNAJA2

DNAJA2, also known as Hdj3, is a human gene that encodes a member of the heat shock protein 40 (Hsp40) family, also known as the DnaJ protein family. These proteins are highly conserved and are involved in a wide range of cellular processes, primarily related to protein folding, protein complex assembly, and protein trafficking. DNAJA2 functions as a co-chaperone to Hsp70, modulating its ATPase activity and substrate binding.

Functionally, DNAJA2 assists Hsp70 in recognizing and binding to unfolded or misfolded proteins, preventing their aggregation and promoting proper folding. It contains a J domain, which is a hallmark of the DnaJ family and is crucial for stimulating Hsp70’s ATPase activity. This interaction allows Hsp70 to stabilize the substrate protein. Beyond its general chaperone function, DNAJA2 is implicated in specific cellular pathways and disease processes.

DNAJA2 is expressed in various tissues, often at different levels depending on cellular stress or developmental stage. Studies suggest its involvement in processes such as cell proliferation, apoptosis, and response to oxidative stress. Misregulation or mutations in DNAJA2 have been linked to various diseases, including certain types of cancer. Specifically, altered expression levels and functional impairments of DNAJA2 have been observed in some tumors, suggesting a role in tumor progression and metastasis.

Research continues to explore the precise mechanisms and roles of DNAJA2 in cellular homeostasis and disease, making it a target for potential therapeutic interventions.