Mitochondrial heat shock protein 70 (MtHsp70; often formally "Heat shock 70 kDa protein 9, mitochondrial") (HSPA9 (also GRP75, mortalin))

Mitochondrial heat shock protein 70 (MtHsp70, also called HSPA9/GRP75/mortalin) is a major member of the heat shock protein 70 superfamily and serves as a critical ATP-dependent molecular chaperone in mitochondria. MtHsp70 facilitates the import of nuclear-encoded mitochondrial proteins and assists their folding, thereby maintaining mitochondrial proteostasis. It participates in mitochondrial DNA replication and maintenance, supports cellular viability under stress, and plays a role in the regulation of apoptosis and mitochondrial dynamics[1][2][4][9]. Dysregulation or overexpression of MtHsp70 has been linked to cancer, neurodegenerative disorders, and mitochondrial diseases. The unique abundance and stress-inducibility of mitochondrial Hsp70 in malignant tissues make it an emerging cancer therapy target, with several small molecules developed to inhibit its function and promote selective apoptosis in tumor cells[2][4].

Other names

GRP75MortalinHSPA9Heat shock 70 kDa protein 9Heat shock protein family A member 9mtHsp70

Inhibition of chaperone function, leading to impaired protein folding and aggregation; Disruption of mitochondrial protein import; Induction of apoptosis via mitochondrial dysfunction and altered dynamics; Inhibition of mitochondrial DNA maintenance[2][4]; Modulation of cellular stress responses