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Neurosci Res. 2010 Jan;66(1):131-3. doi: 10.1016/j.neures.2009.10.004. Epub 2009 Oct 13.

The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases.

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  • 1Department of Clinical Neurology and Stroke Medicine, Graduate School of Medicine, Yokohama City University, 3-9 Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan. doi@rkd.d-bs.com

Abstract

Neuronal intranuclear inclusions (NIIs) are the pathological hallmark of polyglutamine (polyQ) diseases. We previously found that the RNA-binding protein FUS/TLS is the major component of nuclear polyQ aggregates of a cellular model of Huntington disease. In this study, we revealed that FUS/TLS binds to NIIs in the human brains from patients with spinocerebellar ataxia type 1, 2, 3, and dentatorubral-pallidoluysian atrophy. Recent reports have revealed that mutations in FUS/TLS gene are responsible for familial amyotrophic lateral sclerosis 6 (ALS6). Our results indicated that changing FUS/TLS to an insoluble form may be a common process in polyQ diseases and ALS6.

Copyright 2009 Elsevier Ireland Ltd and the Japan Neuroscience Society. All rights reserved.

PMID:
19833157
[PubMed - indexed for MEDLINE]
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