| http://purl.uniprot.org/citations/21186323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21186323 | http://www.w3.org/2000/01/rdf-schema#comment | "Costameres are cellular sites of mechanotransduction in heart and skeletal muscle where dystrophin and its membrane-spanning partner dystroglycan distribute intracellular contractile forces into the surrounding extracellular matrix. Resolution of a functional costamere interactome is still limited but likely to be critical for understanding forms of muscular dystrophy and cardiomyopathy. Dystrophin binds a set of membrane-associated proteins (the dystrophin-glycoprotein complex) as well as γ-actin and microtubules and also is required to align sarcolemmal microtubules with costameres. Ankyrin-B binds to dystrophin, dynactin-4, and microtubules and is required for sarcolemmal association of these proteins as well as dystroglycan. We report here that ankyrin-B interactions with β2 spectrin and dynactin-4 are required for localization of dystrophin, dystroglycan, and microtubules at costameres as well as protection of muscle from exercise-induced injury. Knockdown of dynactin-4 in adult mouse skeletal muscle phenocopied depletion of ankyrin-B and resulted in loss of sarcolemmal dystrophin, dystroglycan, and microtubules. Moreover, mutations of ankyrin-B and of dynactin-4 that selectively impaired binary interactions between these proteins resulted in loss of their costamere-localizing activity and increased muscle fiber fragility as a result of loss of costamere-associated dystrophin and dystroglycan. In addition, costamere-association of dynactin-4 did not require dystrophin but did depend on β2 spectrin and ankyrin-B, whereas costamere association of ankyrin-B required β2 spectrin. Together, these results are consistent with a functional hierarchy beginning with β2 spectrin recruitment of ankyrin-B to costameres. Ankyrin-B then interacts with dynactin-4 and dystrophin, whereas dynactin-4 collaborates with dystrophin in coordinating costamere-aligned microtubules."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.187831"xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/author | "Hoffman J."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/author | "Bennett V."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/author | "Ayalon G."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/author | "Davis J.Q."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/author | "Kizhatil K."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/author | "Hostettler J.D."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/pages | "7370-7378"xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/title | "Ankyrin-B interactions with spectrin and dynactin-4 are required for dystrophin-based protection of skeletal muscle from exercise injury."xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://purl.uniprot.org/core/volume | "286"xsd:string |
| http://purl.uniprot.org/citations/21186323 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21186323 |
| http://purl.uniprot.org/citations/21186323 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21186323 |
| http://purl.uniprot.org/uniprot/#_A0A023ZT56-mappedCitation-21186323 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21186323 |
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