RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/21081650http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21081650http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21081650http://www.w3.org/2000/01/rdf-schema#comment"Increasing evidence indicates that cellular uptake of several molecules can occur independently of functional dynamin, but the molecular players that regulate dynamin-independent endocytosis and the subsequent trafficking steps are still largely unknown. A survival-based short-hairpin (sh) RNA screen using a cell line expressing a diphtheria toxin receptor (DTR, officially known as HBEGF) anchored to GPI (DTR-GPI), which internalizes diphtheria toxin (DT, officially known as DTX) in a dynamin-independent manner, identified PI3KC2α, a class II phosphoinositide 3-kinase (PI3K), as a specific regulator of dynamin-independent DT internalization. We found that the internalization of several proteins that enter the cell through dynamin-independent pathways led to a relocalization of PI3KC2α to cargo-positive vesicles. Furthermore, downregulation of PI3KC2α impaired internalization of CD59 as well as fluid-phase endocytosis. Our data suggest a general role for PI3KC2α in regulating physiologically relevant dynamin-independent internalization pathways by recruiting early endosome antigen 1 (EEA1) to vesicular compartments, a step required for the intracellular trafficking of vesicles generated by dynamin-independent endocytic pathways."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.org/dc/terms/identifier"doi:10.1242/jcs.071712"xsd:string
http://purl.uniprot.org/citations/21081650http://purl.org/dc/terms/identifier"doi:10.1242/jcs.071712"xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/author"Salcini A.E."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/author"Salcini A.E."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/author"Malmberg E.K."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/author"Malmberg E.K."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/author"Krag C."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/author"Krag C."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/pages"4240-4250"xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/pages"4240-4250"xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/title"PI3KC2alpha, a class II PI3K, is required for dynamin-independent internalization pathways."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/title"PI3KC2alpha, a class II PI3K, is required for dynamin-independent internalization pathways."xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/volume"123"xsd:string
http://purl.uniprot.org/citations/21081650http://purl.uniprot.org/core/volume"123"xsd:string
http://purl.uniprot.org/citations/21081650http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21081650
http://purl.uniprot.org/citations/21081650http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21081650
http://purl.uniprot.org/citations/21081650http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21081650
http://purl.uniprot.org/citations/21081650http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21081650