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http://purl.uniprot.org/citations/26446751http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26446751http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26446751http://www.w3.org/2000/01/rdf-schema#comment"In striated muscle, X-ROS is the mechanotransduction pathway by which mechanical stress transduced by the microtubule network elicits reactive oxygen species. X-ROS tunes Ca(2+) signalling in healthy muscle, but in diseases such as Duchenne muscular dystrophy (DMD), microtubule alterations drive elevated X-ROS, disrupting Ca(2+) homeostasis and impairing function. Here we show that detyrosination, a post-translational modification of α-tubulin, influences X-ROS signalling, contraction speed and cytoskeletal mechanics. In the mdx mouse model of DMD, the pharmacological reduction of detyrosination in vitro ablates aberrant X-ROS and Ca(2+) signalling, and in vivo it protects against hallmarks of DMD, including workload-induced arrhythmias and contraction-induced injury in skeletal muscle. We conclude that detyrosinated microtubules increase cytoskeletal stiffness and mechanotransduction in striated muscle and that targeting this post-translational modification may have broad therapeutic potential in muscular dystrophies."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.org/dc/terms/identifier"doi:10.1038/ncomms9526"xsd:string
http://purl.uniprot.org/citations/26446751http://purl.org/dc/terms/identifier"doi:10.1038/ncomms9526"xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Harki D.A."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Harki D.A."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Shi G."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Shi G."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Ward C.W."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Ward C.W."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Prosser B.L."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Prosser B.L."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Bogush A.I."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Bogush A.I."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Robison P."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Robison P."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Martin S.S."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Martin S.S."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Becerra N."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Becerra N."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Hexum J.K."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Hexum J.K."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Kempema A.M."xsd:string
http://purl.uniprot.org/citations/26446751http://purl.uniprot.org/core/author"Kempema A.M."xsd:string