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http://purl.uniprot.org/citations/16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16638567http://www.w3.org/2000/01/rdf-schema#comment"Annexin A8 is a poorly characterized member of the annexin family of Ca2+-regulated membrane binding proteins. Initially only identified at the cDNA level it had been tentatively linked to acute promyelocytic leukaemia (APL) due to its high and regulated expression in APL-derived cells. Here we identify unique properties of the annexin A8 protein. We show that it binds Ca2+-dependently and with high specificity to phosphatidylinositol (4,5)-bisphosphate (PtdIns(4,5)P2) and is also capable of interacting with F-actin. In line with these characteristics annexin A8 is recruited to F-actin-associated PtdIns(4,5)P2-rich membrane domains formed in HeLa cells upon infection with non-invading enteropathogenic Escherichia coli. These properties suggest a role of annexin A8 in the organization of certain actin-associated membrane domains."xsd:string
http://purl.uniprot.org/citations/16638567http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2006.03.076"xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/author"Gerke V."xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/author"Goebeler V."xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/author"Rescher U."xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/author"Ruhe D."xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/pages"2430-2434"xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/title"Annexin A8 displays unique phospholipid and F-actin binding properties."xsd:string
http://purl.uniprot.org/citations/16638567http://purl.uniprot.org/core/volume"580"xsd:string
http://purl.uniprot.org/citations/16638567http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16638567
http://purl.uniprot.org/citations/16638567http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16638567
http://purl.uniprot.org/uniprot/P13928#attribution-D31A484044533E582A26CD2F070B8BCFhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/#_A0A087WTN9-mappedCitation-16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/#_P13928-mappedCitation-16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/#_B4DQE1-mappedCitation-16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/#_B4DTB3-mappedCitation-16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/#_B4DLF6-mappedCitation-16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/#_P68135-mappedCitation-16638567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/B4DQE1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/P13928http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/A0A087WTN9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16638567
http://purl.uniprot.org/uniprot/B4DLF6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16638567