RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/12660155http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12660155http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12660155http://www.w3.org/2000/01/rdf-schema#comment"TRPV5 and TRPV6 constitute the Ca(2+) influx pathway in a variety of epithelial cells. Here, we identified S100A10 as the first auxiliary protein of these epithelial Ca(2+) channels using yeast two-hybrid and GST pull-down assays. This S100 protein forms a heterotetrameric complex with annexin 2 and associates specifically with the conserved sequence VATTV located in the C-terminal tail of TRPV5 and TRPV6. Of these five amino acids, the first threonine plays a crucial role since the corresponding mutants (TRPV5 T599A and TRPV6 T600A) exhibited a diminished capacity to bind S100A10, were redistributed to a subplasma membrane area and did not display channel activity. Using GST pull-down and co-immunoprecipitation assays we demonstrated that annexin 2 is part of the TRPV5-S100A10 complex. Furthermore, the S100A10-annexin 2 pair colocalizes with the Ca(2+) channels in TRPV5-expressing renal tubules and TRPV6-expressing duodenal cells. Importantly, downregulation of annexin 2 using annexin 2-specific small interfering RNA inhibited TRPV5 and TRPV6-mediated currents in transfected HEK293 cells. In conclusion, the S100A10-annexin 2 complex plays a crucial role in routing of TRPV5 and TRPV6 to plasma membrane."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg162"xsd:string
http://purl.uniprot.org/citations/12660155http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg162"xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Gerke V."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Gerke V."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Staub O."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Staub O."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Hoenderop J.G."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Hoenderop J.G."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Rescher U."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Rescher U."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"van de Graaf S.F."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"van de Graaf S.F."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Bindels R.J.M."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Bindels R.J.M."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Nilius B."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Nilius B."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Prenen J."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Prenen J."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Gkika D."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Gkika D."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Lamers D."xsd:string
http://purl.uniprot.org/citations/12660155http://purl.uniprot.org/core/author"Lamers D."xsd:string