Work

Reconstructing the Hsp90/Tau Machine

Year: 2013

Type: article

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 contributes 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.

Source: Current Enzyme Inhibition

DOI: 10.2174/1573408011309010006

Authors: Umesh K. Jinwal, John Koren III, Chad A. Dickey

Institutions: University of South Florida, USF Health Byrd Alzheimer's Institute

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Alzheimer's Drug Discovery Foundation, CurePSP, National Institutes of Health, National Institute of Neurological Disorders and Stroke