http://purl.uniprot.org/citations/15294159 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15294159 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15294159 | http://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/15294159 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2004.07.014"xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2004.07.014"xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Barral J.M."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Barral J.M."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Cassata G."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Cassata G."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Baumeister R."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Baumeister R."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Epstein H.F."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Epstein H.F."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Hoppe T."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Hoppe T."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Hutagalung A.H."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Hutagalung A.H."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Springer W."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/author | "Springer W."xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/pages | "337-349"xsd:string |
http://purl.uniprot.org/citations/15294159 | http://purl.uniprot.org/core/pages | "337-349"xsd:string |