RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/23138569http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23138569http://www.w3.org/2000/01/rdf-schema#comment"β-Catenin is essential for muscle development because it regulates both cadherin-mediated cell-cell adhesion and canonical Wingless and Int1 (Wnt) signaling. The phosphorylation of β-catenin by glycogen synthase kinase-3β (GSK-3β) at serine31/37/threonine41 regulates its stability and its role in canonical Wnt signaling. In this study, we have investigated whether the N-terminal phosphorylation of β-catenin is regulated by M-cadherin, and whether this regulation mediates the role of M-cadherin in myogenic differentiation. Our data show that the knockdown of M-cadherin expression by RNA interference (RNAi) in C2C12 myoblasts significantly increases the phosphorylation of β-catenin at Ser33/37/Thr41 and decreases the protein abundance of ser37/thr41-unphosphorylated active β-catenin. Furthermore, M-cadherin RNAi promotes TCF/LEF transcription activity but also blunts the initiation of the myogenic progress by Wnt pathway activator lithium chloride or Wnt-3a treatment. Knockdown of β-catenin expression by RNAi decreases myogenic induction in myoblasts. Forced expression of a phosphorylation-resistant β-catenin plasmid (S33Y-β-catenin) fails to enhance myogenic differentiation, but it partially rescues C2C12 cells from M-cadherin RNAi-induced apoptosis. These data show, for the first time, that M-cadherin-mediated signaling attenuates β-catenin phosphorylation at Ser31/37/Thr41 by GSK-3β, and that this regulation has a positive effect on myogenic differentiation induced by canonical Wnt signaling."xsd:string
http://purl.uniprot.org/citations/23138569http://purl.org/dc/terms/identifier"doi:10.1007/s00441-012-1515-4"xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/author"Mohamed J.S."xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/author"Alway S.E."xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/name"Cell Tissue Res"xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/pages"183-200"xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/title"M-cadherin-inhibited phosphorylation of ss-catenin augments differentiation of mouse myoblasts."xsd:string
http://purl.uniprot.org/citations/23138569http://purl.uniprot.org/core/volume"351"xsd:string
http://purl.uniprot.org/citations/23138569http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23138569
http://purl.uniprot.org/citations/23138569http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23138569
http://purl.uniprot.org/uniprot/#_Q02248-mappedCitation-23138569http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23138569
http://purl.uniprot.org/uniprot/#_P33146-mappedCitation-23138569http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23138569
http://purl.uniprot.org/uniprot/P33146http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23138569
http://purl.uniprot.org/uniprot/Q02248http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23138569