Abstract
The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). However, there is little information to date about the upstream proteins in the ubiquitin-proteasome system of pathogenic ataxin3-80Q. Here, we report that BAG2 (Bcl-2 associated athanogene family protein 2) and BAG5 (Bcl-2-associated athanogene family protein 5) stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination as determined based on western blotting and co-immunofluorescence experiments. The association of the BAG2 and BAG5 proteins with pathogenic ataxin3-80Q strengthens the important roles of the BAG family in neurodegenerative diseases.
Keywords:
BAG2; BAG5; pathogenic ataxin3-80Q; spinocerebellar ataxia type-3; ubiquitin-proteasome system.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism*
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Analysis of Variance
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Ataxin-3 / genetics
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Ataxin-3 / metabolism*
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Gene Expression Regulation / genetics
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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HEK293 Cells
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Humans
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Immunoprecipitation
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism*
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Peptides / genetics
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Peptides / metabolism*
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Transfection
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Ubiquitination / physiology*
Substances
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Adaptor Proteins, Signal Transducing
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BAG2 protein, human
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BAG5 protein, human
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Molecular Chaperones
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Peptides
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Repressor Proteins
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enhanced green fluorescent protein
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Green Fluorescent Proteins
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polyglutamine
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ATXN3 protein, human
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Ataxin-3