NDLI: Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis.

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Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis.

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Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Miller, Victor M. Williams, Aislinn Shao, Jianqiang Paulson, Henry L. Chai, Yaohui
Description	Author Affiliation: Chai Y ( Department of Neurology, 3160 Medical Labs, University of Iowa College of Medicine, Iowa City, IA 52242, USA.);
Abstract	Protein misfolding and aggregation are central features of the polyglutamine neurodegenerative disorders, but the dynamic properties of expanded polyglutamine proteins are poorly understood. Here, we use fluorescence recovery after photobleaching (FRAP) and fluorescence loss in photobleaching (FLIP) with green fluorescent protein fusion proteins to study polyglutamine protein kinetics in living cells. Our results reveal markedly divergent mobility states for an expanded polyglutamine protein, ataxin-3, and establish that nuclear inclusions formed by this protein are aggregates. Additional studies of green fluorescent protein-tagged cAMP response element binding protein coexpressed with either of two mutant polyglutamine proteins, ataxin-3 and huntingtin, support a model of disease in which coaggregation of transcriptional components contributes to pathogenesis. Finally, studies of a third polyglutamine disease protein, ataxin-1, reveal unexpected heterogeneity in the dynamics of inclusions formed by different disease proteins, a finding which may help explain disease-specific elements of pathogenesis in these neurodegenerative disorders.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Heredodegenerative Disorders, Nervous System Genetics Metabolism Nerve Tissue Proteins Peptides Animals Ataxin-3 COS Cells CREB-Binding Protein Green Fluorescent Proteins Etiology Luminescent Proteins Models, Neurological Mutation Nuclear Proteins Recombinant Fusion Proteins Repressor Proteins Trans-Activators Transfection Trinucleotide Repeats Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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