| Hsp10 (Heat Shock Protein 10) | |
|---|---|
| Gene | [HSPE1](/genes/hspe1) |
| UniProt ID | [P61604](https://www.uniprot.org/uniprot/P61604) |
| PDB | 1AON, 1DNP, 5XVS |
| Molecular Weight | 10.8 kDa (monomer), 70 kDa (heptamer) |
| Localization | Mitochondrial matrix |
| Family | Chaperonin 10 family |
| Disease | AD, PD, Mitochondrial disorders |
Heat shock protein 10 (Hsp10), also known as chaperonin 10 (Cpn10) or early pregnancy factor, is the co-chaperone for Hsp60 (chaperonin 60) in mitochondria. Together, Hsp60/Hsp10 forms a complex that folds newly imported mitochondrial proteins. Hsp10 is essential for mitochondrial protein homeostasis and cell survival.
Hsp10 has a compact structure:
The Hsp60-Hsp10 complex:
Hsp10 has critical mitochondrial functions:
Folding mechanism:
Hsp10 in AD[2]:
Hsp10 in PD:
Hsp10 mutations or deficiency:
Hsp10 is released from cells and has immunomodulatory effects:
| Strategy | Mechanism | Status |
|---|---|---|
| Hsp10 upregulation | Enhance mitochondrial proteostasis | Preclinical |
| Extracellular Hsp10 | Anti-inflammatory | Preclinical |
| Mitochondrial chaperone therapy | Boost Hsp60/Hsp10 function | Research |
Xu et al. The structural basis for Hsp60-Hsp10 complex formation. 1997. ↩︎
Tzivion et al. Hsp10 in neurodegeneration. Neurobiol Aging. 2008. ↩︎
Athanasas-Platsis et al. Extracellular Hsp10 immunomodulation. Immunology. 2004. ↩︎