Reconstructing the Hsp90/Tau Machine

Title:Reconstructing the Hsp90/Tau Machine

Volume: 9 Issue: 1

Author(s): Umesh K. Jinwal, John Koren III and Chad A. Dickey

Affiliation:

Keywords: Alzheimer’s disease, microtubule associated protein tau, chaperone, Heat shock protein, Hsp90, co-chaperone.

Abstract: Imbalanced protein load within cells is a critical aspect for most diseases of aging. In particular, the accumulation of proteins into neurotoxic aggregates is a common thread for a host of neurodegenerative diseases. Recent work demonstrates that age-related changes to the cellular chaperone repertoire contribute to abnormal buildup of the microtubule- associated protein tau that accumulates in a group of diseases termed tauopathies, the most common being Alzheimer’s disease (AD). The Hsp90 co-chaperone repertoire has diverse effects on tau stability; some co-chaperones stabilize tau while others facilitate its clearance. We propose that each of these proteins may be novel therapeutic targets. While targeting Hsp90 directly may be deleterious at the organismal level, perhaps targeting individual co-chaperone activities will be more tolerable.

Cite this article as:

K. Jinwal Umesh, Koren III John and A. Dickey Chad, Reconstructing the Hsp90/Tau Machine, Current Enzyme Inhibition 2013; 9 (1) . https://dx.doi.org/10.2174/1573408011309010006