10 kDa heat shock protein, mitochondrial

HSPE1 encodes the 10 kDa heat shock protein (Hsp10), a mitochondrial co-chaperonin that facilitates protein folding and assembly within the mitochondrial matrix (UniProt: P61604). Working in conjunction with Hsp60, Hsp10 forms part of a chaperonin complex that prevents misfolding and promotes refolding of imported proteins and those generated under stress conditions, sequestering substrates in a protected cavity during the folding cycle.

As a mitochondrial chaperone, HSPE1 functions in maintaining protein homeostasis and cellular stress responses—processes critical to mitochondrial bioenergetics and cellular viability across tissues.

HSPE1 is associated with Alzheimer's Disease and shows consistent downregulation in post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics). The mean log2 fold-change is −0.35 across the measured fraction, suggesting a modest but reproducible reduction in this co-chaperonin in AD pathology. Decreased mitochondrial chaperone capacity may contribute to impaired protein quality control and mitochondrial dysfunction observed in AD neurodegeneration.