Reconstructing the Hsp90/Tau Machine

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

Journal Name: Current Enzyme Inhibition

Volume 9 , Issue 1 , 2013

Become EABM
Become Reviewer


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.

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

promotion: free to download

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2013
Page: [41 - 45]
Pages: 5
DOI: 10.2174/1573408011309010006

Article Metrics

PDF: 26