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http://purl.uniprot.org/citations/15294159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15294159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15294159http://www.w3.org/2000/01/rdf-schema#comment"The organization of the motor protein myosin into motile cellular structures requires precise temporal and spatial control. Caenorhabditis elegans UNC-45 facilitates this by functioning both as a chaperone and as a Hsp90 cochaperone for myosin during thick filament assembly. Consequently, mutations in C. elegans unc-45 result in paralyzed animals with severe myofibril disorganization in striated body wall muscles. Here, we report a new E3/E4 complex, formed by CHN-1, the C. elegans ortholog of CHIP (carboxyl terminus of Hsc70-interacting protein), and UFD-2, an enzyme known to have ubiquitin conjugating E4 activity in yeast, as necessary and sufficient to multiubiquitylate UNC-45 in vitro. The phenotype of unc-45 temperature-sensitive animals is partially suppressed by chn-1 loss of function, while UNC-45 overexpression in worms deficient for chn-1 results in severely disorganized muscle cells. These results identify CHN-1 and UFD-2 as a functional E3/E4 complex and UNC-45 as its physiologically relevant substrate."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2004.07.014"xsd:string
http://purl.uniprot.org/citations/15294159http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2004.07.014"xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Barral J.M."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Barral J.M."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Cassata G."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Cassata G."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Baumeister R."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Baumeister R."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Epstein H.F."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Epstein H.F."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Hoppe T."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Hoppe T."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Hutagalung A.H."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Hutagalung A.H."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Springer W."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/author"Springer W."xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/pages"337-349"xsd:string
http://purl.uniprot.org/citations/15294159http://purl.uniprot.org/core/pages"337-349"xsd:string