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Author Notes:

Correspondence: Xiao-Jiang Li: xli2@emory.edu

Authors' Contributions: LSH, SHL, and XJL wrote the manuscript.

All authors read and approved the final manuscript.

Disclosures: The authors declare that they have no competing interests.


Research Funding:

The work from the authors' laboratory was supported by grants from the NIH (AG019206, NS036232, NS041669).

Nuclear accumulation of polyglutamine disease proteins and neuropathology


Journal Title:

Molecular Brain


Volume 2, Number 21


, Pages 1-7

Type of Work:

Article | Final Publisher PDF


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.

Copyright information:

© 2009 Havel et al; licensee BioMed Central Ltd.

This is an Open Access work distributed under the terms of the Creative Commons Attribution 2.0 Generic License (http://creativecommons.org/licenses/by/2.0/).

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