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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2009-4-6
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pubmed:abstractText |
Huntington disease and its related autosomal-dominant polyglutamine (pQ) neurodegenerative diseases are characterized by intraneuronal accumulation of protein aggregates. Studies on protein aggregates have revealed the importance of the ubiquitin-proteasome system as the front line of protein quality control (PQC) machinery against aberrant proteins. Recently, we have shown that the autophagy-lysosomal system is also involved in cytoplasmic aggregate degradation, but the nucleus lacked this activity. Consequently, the nucleus relies entirely on the ubiquitin-proteasome system for PQC. According to previous studies, nuclear aggregates possess a higher cellular toxicity than do their cytoplasmic counterparts, however degradation kinetics of nuclear aggregates have been poorly understood. Here we show that nuclear ubiquitin ligases San1p and UHRF-2 each enhance nuclear pQ aggregate degradation and rescued pQ-induced cytotoxicity in cultured cells and primary neurons. Moreover, UHRF-2 is associated with nuclear inclusion bodies in vitro and in vivo. Our data suggest that UHRF-2 is an essential molecule for nuclear pQ degradation as a component of nuclear PQC machinery in mammalian cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-10500182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-10514377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-10581028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-10845064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-10973244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-10984098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-11121744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-11375494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-12058012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-12191472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-12372280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-12612445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-12838312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-14741369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-14993289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-15272267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-15797381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-16141322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-16155577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-16192271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-17067204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-17658611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-17673620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-17687326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-18288205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-2645298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-7984243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-8136840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-8358429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9267034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9620770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9759494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9768849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9778246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9864362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218238-9880673
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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 |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9796-803
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pubmed:dateRevised |
2010-9-23
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pubmed:meshHeading |
pubmed-meshheading:19218238-Cell Nucleus,
pubmed-meshheading:19218238-Cells, Cultured,
pubmed-meshheading:19218238-Cytoplasm,
pubmed-meshheading:19218238-HeLa Cells,
pubmed-meshheading:19218238-Humans,
pubmed-meshheading:19218238-Kinetics,
pubmed-meshheading:19218238-Neurodegenerative Diseases,
pubmed-meshheading:19218238-Neurons,
pubmed-meshheading:19218238-Peptides,
pubmed-meshheading:19218238-Proteasome Endopeptidase Complex,
pubmed-meshheading:19218238-RNA Interference,
pubmed-meshheading:19218238-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:19218238-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:19218238-Ubiquitin,
pubmed-meshheading:19218238-Ubiquitin-Protein Ligases
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pubmed:year |
2009
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pubmed:articleTitle |
Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system.
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pubmed:affiliation |
Departments of Molecular Neuroscience on Neurodegeneration and Neurology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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