Functional significance of minor structural and expression changes in stress chaperone mortalin

Abstract

Mortalin is one of the highly conserved heat-shock chaperones. Some of the established features of mortalin include its various subcellular localizations, multiple binding partners, and differential subcellular distribution in normal and immortal cells. It inhibits nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53. It also functions as an adaptive protein in a variety of stress-response mechanisms and contributes to human carcinogenesis. Interestingly, minor alterations in its structure and level of expression may lead to drastic biological consequences (for example, Myelodysplastic syndrome and old age pathologies, such as Alzheimer's and Parkinson's disease). Besides being validated as a reliable target for cancer therapy, mortalin also warrants attention from the perspectives of management of old-age diseases and healthy aging.