Chaperonin heat-shock protein 60 (HSP60)

Chaperonin heat-shock protein 60 (HSP60) is an essential, highly conserved molecular chaperone mainly localized in mitochondria, where it forms a complex with cochaperonin HSP10 to mediate the ATP-dependent folding and assembly of newly synthesized and stress-unfolded proteins, thereby maintaining cellular protein homeostasis and mitochondrial function[1][2][3][4]. HSP60 consists of 60 kDa subunits that oligomerize into ring-shaped structures to encapsulate substrate proteins in a unique folding chamber, preventing aggregation and facilitating correct folding[1][2][3]. Beyond its canonical chaperone activities, HSP60 also participates in apoptotic regulation, immunity, cell proliferation, and is associated with diverse pathologies when dysregulated, including cancer, cardiovascular disease, neurodegenerative disorders, infections, and so-called chaperonopathies[2][4]. HSP60 is also found outside mitochondria in the cytoplasm, cell membrane, and extracellular space, where it can act as a pro-inflammatory danger signal[4]. Its central roles in protein quality control make it an emerging therapeutic target, though fundamental physiological functions pose challenges for safe pharmacological intervention.

Other names

Heat shock protein 60HSP6060 kDa chaperoninChaperonin 60Cpn60Mitochondrial chaperonin Hsp60mHsp60

ATP-dependent folding of mitochondrial and cytosolic proteins Prevention of apoptosis under stress conditions Drugs may inhibit chaperone activity or disrupt protein-protein interactions