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http://purl.uniprot.org/citations/23283987http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23283987http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23283987http://www.w3.org/2000/01/rdf-schema#comment"We identify cpna-1 (F31D5.3) as a novel essential muscle gene in the nematode Caenorhabditis elegans. Antibodies specific to copine domain protein atypical-1 (CPNA-1), as well as a yellow fluorescent protein translational fusion, are localized to integrin attachment sites (M-lines and dense bodies) in the body-wall muscle of C. elegans. CPNA-1 contains an N-terminal predicted transmembrane domain and a C-terminal copine domain and binds to the M-line/dense body protein PAT-6 (actopaxin) and the M-line proteins UNC-89 (obscurin), LIM-9 (FHL), SCPL-1 (SCP), and UNC-96. Proper CPNA-1 localization is dependent upon PAT-6 in embryonic and adult muscle. Nematodes lacking cpna-1 arrest elongation at the twofold stage of embryogenesis and display disruption of the myofilament lattice. The thick-filament component myosin heavy chain MYO-3 and the M-line component UNC-89 are initially localized properly in cpna-1-null embryos. However, in these embryos, when contraction begins, MYO-3 and UNC-89 become mislocalized into large foci and animals die. We propose that CPNA-1 acts as a linker between an integrin-associated protein, PAT-6, and membrane-distal components of integrin adhesion complexes in the muscle of C. elegans."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e12-06-0478"xsd:string
http://purl.uniprot.org/citations/23283987http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e12-06-0478"xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Xiong G."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Xiong G."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Qadota H."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Qadota H."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Benian G.M."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Benian G.M."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Moerman D.G."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Moerman D.G."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Warner A."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Warner A."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Rogalski T."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Rogalski T."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Vogl A.W."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/author"Vogl A.W."xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/pages"601-616"xsd:string
http://purl.uniprot.org/citations/23283987http://purl.uniprot.org/core/pages"601-616"xsd:string