pubmed-article:17369820 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C0026848 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C1421437 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C1414357 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
pubmed-article:17369820 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
pubmed-article:17369820 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:17369820 | pubmed:dateCreated | 2007-4-2 | lld:pubmed |
pubmed-article:17369820 | pubmed:abstractText | Protein degradation in eukaryotes often requires the ubiquitin-selective chaperone p97 for substrate recruitment and ubiquitin-chain assembly. However, the physiological relevance of p97, and its role in developmental processes, remain unclear. Here, we discover an unanticipated function for CDC-48/p97 in myosin assembly and myofibril organization, both in Caenorhabditis elegans and humans. The developmentally regulated assembly of a CDC-48-UFD-2-CHN-1 complex links turnover of the myosin-directed chaperone UNC-45 to functional muscle formation. Our data suggest a similarly conserved pathway regulating myosin assembly in humans. Remarkably, mutations in human p97, known to cause hereditary inclusion-body myopathy, abrogate UNC-45 degradation and result in severely disorganized myofibrils, detrimental towards sarcomeric function. These results identify a key role for CDC-48/p97 in the process of myofibre differentiation and maintenance, which is abolished during pathological conditions leading to protein aggregation and inclusion-body formation in human skeletal muscle. | lld:pubmed |
pubmed-article:17369820 | pubmed:language | eng | lld:pubmed |
pubmed-article:17369820 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17369820 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17369820 | pubmed:month | Apr | lld:pubmed |
pubmed-article:17369820 | pubmed:issn | 1465-7392 | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:CassataGiusep... | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:LochmüllerHan... | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:KrauseSabineS | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:HoppeThorsten... | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:MouyssetJulie... | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:JanieschPhili... | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:KimJohnnyJ | lld:pubmed |
pubmed-article:17369820 | pubmed:author | pubmed-author:BarikbinRojaR | lld:pubmed |
pubmed-article:17369820 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17369820 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:17369820 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17369820 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17369820 | pubmed:pagination | 379-90 | lld:pubmed |
pubmed-article:17369820 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:17369820 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17369820 | pubmed:articleTitle | The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to human myopathy. | lld:pubmed |
pubmed-article:17369820 | pubmed:affiliation | Centre for Molecular Neurobiology (ZMNH), University of Hamburg, Falkenried 94, 20251 Hamburg, Germany. | lld:pubmed |
pubmed-article:17369820 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17369820 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:17369820 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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