Heat shock 70 kDa protein 4 (HSPA4)

Heat shock 70 kDa protein 4 (HSPA4) is a molecular chaperone belonging to the heat shock protein family, primarily involved in protein folding, assembly, and cellular stress response. Originally classified in the HSP70 subgroup but now recognized as a member of the HSP110/etchaperone family, HSPA4 maintains protein homeostasis and facilitates correct folding of polypeptides, especially under stress. HSPA4 is widely expressed and participates in critical processes including cell cycle regulation, apoptosis, DNA repair, and immune modulation. Genomic alterations and dysregulated expression of HSPA4 are implicated in cancer initiation and progression, and it has been suggested as a potential biomarker for cancer prognosis and as a candidate for targeted cancer therapy or immunotherapy. Current research also links HSPA4 to inflammatory diseases, metabolic disorders, and ischemic pathologies.

Other names

HSPA4APG-2APG2Heat shock 70-related protein APG-2HSP70RYHeat shock protein family H member 2HSPH2

Not established for marketed drugs; potential mechanisms inferred for future inhibitors include inhibition of protein folding chaperone activity, disruption of cancer cell proliferation, apoptosis induction, and influence on immune checkpoint activities