| Hsp60 (Heat Shock Protein 60) | |
|---|---|
| Gene | [HSPD1](/genes/hspd1) |
| UniProt ID | [P10809](https://www.uniprot.org/uniprot/P10809) |
| PDB | 1AON, 4PKC, 6N2Q |
| Molecular Weight | 60.3 kDa (monomer), ~840 kDa (tetradecamer) |
| Localization | Mitochondrial matrix |
| Family | Chaperonin 60 family (GroEL homolog) |
| Disease | SPG13, HLD4, AD, PD, Cancer |
Heat shock protein 60 (Hsp60), also known as chaperonin 60 (Cpn60) or HSPD1, is the mitochondrial homolog of bacterial GroEL. Hsp60 is the central mitochondrial chaperone, forming a double-ring structure that provides an enclosed chamber for ATP-dependent protein folding. It is essential for mitochondrial proteostasis and cell viability.
Hsp60 has a characteristic chaperonin architecture:
The Hsp60-Hsp10 complex[1]:
Hsp60 has essential mitochondrial roles:
Client proteins:
HSPD1 mutations cause autosomal dominant hereditary spastic paraplegia:
More severe HSPD1 mutations cause:
Hsp60 in AD:
Hsp60 in PD:
Hsp60 is paradoxically both tumor-promoting and tumor-suppressing:
| Strategy | Mechanism | Status |
|---|---|---|
| Hsp60 upregulation | Enhance mitochondrial proteostasis | Preclinical |
| Hsp60 inhibitors | (Cancer context) | Preclinical |
| Chaperone therapy | Boost Hsp60/Hsp10 function | Research |
| Hsp60 vaccines | Cancer immunotherapy | Preclinical |
Xu et al. The crystal structure of GroEL-GroES complex. 1997. ↩︎
Hansen et al. HSPD1 mutations in SPG13. Am J Hum Genet. 2002. ↩︎
Chandra et al. Hsp60 in cancer. Cell Stress Chaperones. 2016. ↩︎