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http://purl.uniprot.org/citations/20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20215404http://www.w3.org/2000/01/rdf-schema#comment"Organization of the plasma membrane in polarized epithelial cells is accomplished by the specific localization of transmembrane or membrane-associated proteins, which are often linked to cytoplasmic protein complexes, including the actin cytoskeleton. In this study, we identified Sip1 as a Drosophila orthologue of the ezrin-radixin-moesin (ERM) binding protein 50 (EBP50; also known as the Na(+)/H(+) exchanger regulatory factor NHERF1). In mammals, EBP50/NHERF1 is a scaffold protein required for the regulation of several transmembrane receptors and downstream signal transduction activity. In Drosophila, loss of Sip1 leads to a reduction in Slik kinase protein abundance, loss of Moesin phosphorylation and changes in epithelial structure, including mislocalization of E-cadherin and F-actin. Consistent with these findings, Moesin and Sip1 act synergistically in genetic-interaction experiments, and Sip1 protein abundance is dependent on Moesin. Co-immunoprecipitation experiments indicate that Sip1 forms a complex with both Moesin and Slik. Taken together, these data suggest that Sip1 promotes Slik-dependent phosphorylation of Moesin, and suggests a mechanism for the regulation of Moesin activity within the cell to maintain epithelial integrity."xsd:string
http://purl.uniprot.org/citations/20215404http://purl.org/dc/terms/identifier"doi:10.1242/jcs.059469"xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/author"Formstecher E."xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/author"Fehon R.G."xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/author"Hughes S.C."xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/pages"1099-1107"xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/title"Sip1, the Drosophila orthologue of EBP50/NHERF1, functions with the sterile 20 family kinase Slik to regulate Moesin activity."xsd:string
http://purl.uniprot.org/citations/20215404http://purl.uniprot.org/core/volume"123"xsd:string
http://purl.uniprot.org/citations/20215404http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20215404
http://purl.uniprot.org/citations/20215404http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20215404
http://purl.uniprot.org/uniprot/Q7K5M6#attribution-5270CD324E52ECB2B13584F32A2C29E2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/Q7K5M6#attribution-6E37363639B3DDE1604AD7B2A2D9FE59http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/Q7K5M6#attribution-82589B609105C45FED28604DC8C5DC98http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/Q7K5M6#attribution-8D7FDEBF311E8FA8BFE899A54FBE8A6Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_P15278-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_A0A0B4LFX4-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_A0A0B4LG23-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_A8DZ14-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_C7LAH9-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_A4UZU8-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_M9NG50-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404
http://purl.uniprot.org/uniprot/#_B7YZQ1-mappedCitation-20215404http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20215404