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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
36
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pubmed:dateCreated |
2005-9-9
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pubmed:databankReference |
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pubmed:abstractText |
Spinocerebellar ataxia type 3 is a human neurodegenerative disease resulting from polyglutamine tract expansion. The affected protein, ataxin-3, which contains an N-terminal Josephin domain followed by tandem ubiquitin (Ub)-interacting motifs (UIMs) and a polyglutamine stretch, has been implicated in the function of the Ub proteasome system. NMR-based structural analysis has now revealed that the Josephin domain binds Ub and has a papain-like fold that is reminiscent of that of other deubiquitinases, despite primary sequence divergence but consistent with its deubiqutinating activity. Mutation of the catalytic Cys enhances the stability of a complex between ataxin-3 and polyubiquitinated proteins. This effect depends on the integrity of the UIM region, suggesting that the UIMs are bound to the substrate polyubiquitin during catalysis. We propose that ataxin-3 functions as a polyubiquitin chain-editing enzyme.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-10212987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-10367323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-10406793,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-12857950,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-15571815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-15630566,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-8520220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-8578593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-9274833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-9367762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16118278-9488668
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12700-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16118278-Catalysis,
pubmed-meshheading:16118278-Humans,
pubmed-meshheading:16118278-Models, Molecular,
pubmed-meshheading:16118278-Nerve Tissue Proteins,
pubmed-meshheading:16118278-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:16118278-Nuclear Proteins,
pubmed-meshheading:16118278-Protein Binding,
pubmed-meshheading:16118278-Protein Structure, Quaternary,
pubmed-meshheading:16118278-Protein Structure, Tertiary,
pubmed-meshheading:16118278-Repressor Proteins,
pubmed-meshheading:16118278-Ubiquitin
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pubmed:year |
2005
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pubmed:articleTitle |
Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Cell Biology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06510, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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