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http://purl.uniprot.org/citations/18005662http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18005662http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18005662http://www.w3.org/2000/01/rdf-schema#comment"Epithelial calcium (re)absorption is mediated by TRPV5 and TRPV6 channels. TRPV5 is modulated by the SGK1 kinase, a process requiring the PDZ-domain containing scaffold protein NHERF2. The present study explored whether TRPV6 is similarly regulated by SGKs and the scaffold proteins NHERF1/2. In Xenopus oocytes, SGKs activate TRPV6 by increasing its plasma membrane abundance. Deletion of the putative PDZ binding motif on TRPV6 did not abolish channel activation by SGKs. Furthermore, coexpression of neither NHERF1 nor NHERF2 affected TRPV6 or potentiated the SGKs stimulating effect. The present observations disclose a novel TRPV6 regulatory mechanism which presumably participates in calcium homeostasis."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2007.11.006"xsd:string
http://purl.uniprot.org/citations/18005662http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2007.11.006"xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Lang F."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Lang F."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Boehmer C."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Boehmer C."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Klaus F."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Klaus F."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Palmada M."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Palmada M."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Lindner R."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Lindner R."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Laufer J."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Laufer J."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Kenngott C."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/author"Kenngott C."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/pages"5586-5590"xsd:string
http://purl.uniprot.org/citations/18005662http://purl.uniprot.org/core/pages"5586-5590"xsd:string