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http://purl.uniprot.org/citations/19651769http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19651769http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19651769http://www.w3.org/2000/01/rdf-schema#comment"Clathrin-coated vesicles (CCVs) originating from the trans-Golgi network (TGN) provide a major transport pathway from the secretory system to endosomes/lysosomes. Herein we describe paralogous Sec14 domain-bearing proteins, clavesin 1/CRALBPL and clavesin 2, identified through a proteomic analysis of CCVs. Clavesins are enriched on CCVs and form a complex with clathrin heavy chain (CHC) and adaptor protein-1, major coat components of TGN-derived CCVs. The proteins co-localize with markers of endosomes and the TGN as well as with CHC and adaptor protein-1. A membrane mimic assay using the Sec14 domain of clavesin 1 reveals phosphatidylinositol 3,5-bisphosphate as a specific lipid partner. Phosphatidylinositol 3,5-bisphosphate is localized to late endosomes/lysosomes, and interestingly, isoform-specific knockdown of clavesins in neurons using lentiviral delivery of interfering RNA leads to enlargement of a lysosome-associated membrane protein 1-positive membrane compartment with no obvious influence on the CCV machinery at the TGN. Since clavesins are expressed exclusively in neurons, this new protein family appears to provide a unique neuron-specific regulation of late endosome/lysosome morphology."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.034884"xsd:string
http://purl.uniprot.org/citations/19651769http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.034884"xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Katoh Y."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Katoh Y."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"McPherson P.S."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"McPherson P.S."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Honing S."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Honing S."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Ritter B."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Ritter B."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Blondeau F."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Blondeau F."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Gaffry T."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/author"Gaffry T."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/pages"27646-27654"xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/pages"27646-27654"xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/title"The clavesin family: neuron-specific lipid- and clathrin-binding Sec14 proteins regulating lysosomal morphology."xsd:string
http://purl.uniprot.org/citations/19651769http://purl.uniprot.org/core/title"The clavesin family: neuron-specific lipid- and clathrin-binding Sec14 proteins regulating lysosomal morphology."xsd:string