Nuclear accumulation of polyglutamine disease proteins and neuropathology

• Type of Material: Article
• Authors: Lauren S. Havel, Emory University; Shihua Li, Emory University; Xiao-Jiang Li, Emory University
• Language: English
• Date: 2009-07-03
• Publisher: BioMed Central
• Publication Version: Final Published Version
• Copyright Statement: © 2009 Havel et al; licensee BioMed Central Ltd.
• License: Creative Commons Attribution 2.0 Generic
• Final Published Version (URL): http://www.molecularbrain.com/content/2/1/21
• Title of Journal or Parent Work: Molecular Brain
• ISSN: 1756-6606
• Volume: 2
• Issue: 21
• Start Page: 1
• End Page: 7
• Grant/Funding Information: The work from the authors' laboratory was supported by grants from the NIH (AG019206, NS036232, NS041669).
• Research Categories: Biology, Genetics; Biology, Neuroscience

Abstract

There are nine inherited neurodegenerative disorders caused by polyglutamine (polyQ) expansion in various disease proteins. Although these polyglutamine proteins have different functions and are localized in different subcellular regions, all the polyQ diseases share a common pathological feature: the nuclear accumulation of polyQ disease proteins and the formation of inclusions. The nuclear accumulation of polyQ proteins in turn leads to gene transcriptional dysregulation and neuropathology. Here we will discuss potential mechanisms behind the nuclear accumulation of mutant polyQ proteins, since an understanding of how polyQ proteins accumulate in the nucleus could help elucidate the pathogenesis of these diseases and develop their treatment.