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http://purl.uniprot.org/citations/34932950http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34932950http://www.w3.org/2000/01/rdf-schema#comment"Myoblast fusion is essential for muscle development and regeneration. Yet, it remains poorly understood how mononucleated myoblasts fuse with preexisting fibers. We demonstrate that ERK1/2 inhibition (ERKi) induces robust differentiation and fusion of primary mouse myoblasts through a linear pathway involving RXR, ryanodine receptors, and calcium-dependent activation of CaMKII in nascent myotubes. CaMKII activation results in myotube growth via fusion with mononucleated myoblasts at a fusogenic synapse. Mechanistically, CaMKII interacts with and regulates MYMK and Rac1, and CaMKIIδ/γ knockout mice exhibit smaller regenerated myofibers following injury. In addition, the expression of a dominant negative CaMKII inhibits the formation of large multinucleated myotubes. Finally, we demonstrate the evolutionary conservation of the pathway in chicken myoblasts. We conclude that ERK1/2 represses a signaling cascade leading to CaMKII-mediated fusion of myoblasts to myotubes, providing an attractive target for the cultivated meat industry and regenerative medicine."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2021.11.022"xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Sinha S."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Avinoam O."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Segev N."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Schejter E.D."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Zaritsky A."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Amzallag E."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Tzahor E."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Millay D.P."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Eigler T."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Umansky K.B."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Zarfati G."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Shakked A."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/author"Zabary Y."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/name"Dev Cell"xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/pages"3349-3363.e6"xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/title"ERK1/2 inhibition promotes robust myotube growth via CaMKII activation resulting in myoblast-to-myotube fusion."xsd:string
http://purl.uniprot.org/citations/34932950http://purl.uniprot.org/core/volume"56"xsd:string
http://purl.uniprot.org/citations/34932950http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34932950
http://purl.uniprot.org/citations/34932950http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34932950
http://purl.uniprot.org/uniprot/#_D3Z7K9-mappedCitation-34932950http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34932950
http://purl.uniprot.org/uniprot/#_A0A0G2JGS4-mappedCitation-34932950http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34932950