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http://purl.uniprot.org/citations/11082044http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11082044http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11082044http://www.w3.org/2000/01/rdf-schema#comment"The PACSINs are a family of cytoplasmic phosphoproteins that play a role in vesicle formation and transport. We report the cloning and cDNA sequencing of PACSIN 3 and the analysis of all three PACSIN isoforms with regard to tissue distribution, ligand binding properties and influence on endocytosis. PACSIN 3 differs from the other family members in having a short proline-rich region and lacking asparagine-proline-phenylalanine motifs. In contrast to the neurospecific PACSIN 1 and the ubiquitously expressed PACSIN 2, PACSIN 3 is mainly detected in lung and muscle tissues. All isoforms potentially oligomerize and bind to dynamin, synaptojanin 1 and N-WASP via their Src homology 3 domains. The PACSIN proteins colocalize with dynamin, but not with clathrin, implying a specific role with a distinct subpopulation of dynamin at defined cellular sites. Transferrin endocytosis is blocked in a dose-dependent manner in cells overexpressing the PACSIN variants, but the inhibitory effect can be abolished by mutating specific amino acid residues in the Src homology 3 domains. These characteristics of the PACSIN protein family suggest a general function in recruitment of the interacting proteins to sites of endocytosis."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.org/dc/terms/identifier"doi:10.1242/jcs.113.24.4511"xsd:string
http://purl.uniprot.org/citations/11082044http://purl.org/dc/terms/identifier"doi:10.1242/jcs.113.24.4511"xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Ritter B."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Ritter B."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Modregger J."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Modregger J."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Plomann M."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Plomann M."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Paulsson M."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Paulsson M."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Witter B."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/author"Witter B."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/pages"4511-4521"xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/pages"4511-4521"xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/title"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/title"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis."xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/volume"113"xsd:string
http://purl.uniprot.org/citations/11082044http://purl.uniprot.org/core/volume"113"xsd:string