Heat shock cognate 71 kDa protein (Hsc70)

Heat shock cognate 71 kDa protein (Hsc70, also known as HSPA8) is a constitutively expressed molecular chaperone belonging to the heat shock protein 70 family. It plays a central role in maintaining cellular proteostasis by facilitating proper folding/refolding of newly synthesized or misfolded polypeptides, preventing aggregation under both normal and stressed conditions. It also assists with intracellular trafficking across membranes and targets damaged/mutant proteins for degradation via ubiquitin-proteasome/autophagy pathways. Its functions are critical for processes such as signal transduction regulation, apoptosis control, autophagy initiation, cell growth/differentiation support—and it interacts with numerous co-chaperones including members from the BAG family and other heat-shock partners like Hsp40/Hsp90 complexes. Dysregulation has been implicated in various cancers, neurodegenerative diseases such as Alzheimer’s/Parkinson’s disease, aging/senescence phenomena—and it remains an active area for therapeutic research due to its central role at the intersection between cell survival/death decisions under stress conditions.

Other names

Heat shock 70 kDa protein 8Hsc70Hsp73Hsp71Hsc71Heat shock protein family A member 8HSPA8

Drugs targeting this molecule typically act by inhibiting its ATPase activity or disrupting its interaction with client/co-chaperone proteins. This can lead to accumulation of misfolded proteins and induction of apoptosis in cancer cells or modulation of proteostasis networks.