Hsp70Hsc70
Hsp70 and Hsc70 refer to members of the Hsp70 (heat shock protein 70) chaperone family. The terms are used to distinguish inducible and constitutive cytosolic forms, though the family also includes organelle-specific members. In humans, the constitutive cytosolic Hsc70 is encoded by HSPA8, while inducible cytosolic Hsp70 isoforms include HSPA1A and HSPA1B (often collectively called Hsp70 or Hsp72). Other organelle-specific members include BiP/GRP78 (HSPA5) in the endoplasmic reticulum and mitochondrial Hsp70s (e.g., mortalin, HSPA9).
Hsp70 proteins share a characteristic architecture with an N-terminal ATPase domain and a C-terminal substrate-binding domain,
Hsp70 chaperones assist de novo protein folding, prevent aggregation of unfolded proteins, help translocate proteins across
Hsp70/Hsc70 proteins are central to cellular proteostasis and are upregulated during stress. They are implicated in