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http://purl.uniprot.org/citations/19033387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19033387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19033387http://www.w3.org/2000/01/rdf-schema#comment"The ADP-ribosylation factor 6 (Arf6) GTPase functions as a key regulator of endocytic trafficking, participating in clathrin-independent endocytosis in most cell types. Unexpectedly, we found that siRNA-mediated depletion of clathrin or of adaptor protein 2 (AP-2)-complex subunits alters trafficking of Arf6 pathway cargo proteins, such as major histocompatibility complex class I (MHCI) and beta1 integrin. Internalization of these cargoes from the plasma membrane was not affected in cells depleted of clathrin, but was modestly delayed in cells lacking AP-2. Furthermore, depletion of clathrin or AP-2 altered the intracellular distribution of MHCI and beta1 integrin, inducing clustering in a perinuclear region. Despite this altered localization in both depleted populations, enhanced lysosomal targeting of MHCI was observed uniquely in cells that lack AP-2. Total levels of MHCI were modestly but consistently reduced in AP-2-depleted cells, and restored by the lysosomal inhibitor bafilomycin A. Furthermore, the half-life of surface-derived MHCI was reduced in AP-2-depleted cells. Consistent with enhanced degradative sorting, colocalization of Arf6 cargo with the late endosome and lysosome markers CD63 and Lamp1 was increased in cells depleted of AP-2 but not clathrin. These studies indicate a role for AP-2 in maintaining normal post-endocytic trafficking through the Arf6-regulated, non-clathrin pathway, and reveal pervasive effects of clathrin and AP-2 depletion on the endosomal and lysosomal system."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.org/dc/terms/identifier"doi:10.1242/jcs.033522"xsd:string
http://purl.uniprot.org/citations/19033387http://purl.org/dc/terms/identifier"doi:10.1242/jcs.033522"xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/author"Chou M.M."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/author"Chou M.M."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/author"Lau A.W."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/author"Lau A.W."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/pages"4008-4017"xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/pages"4008-4017"xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/title"The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/title"The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway."xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/volume"121"xsd:string
http://purl.uniprot.org/citations/19033387http://purl.uniprot.org/core/volume"121"xsd:string
http://purl.uniprot.org/citations/19033387http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19033387
http://purl.uniprot.org/citations/19033387http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19033387
http://purl.uniprot.org/citations/19033387http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19033387
http://purl.uniprot.org/citations/19033387http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19033387
http://purl.uniprot.org/uniprot/O95782http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19033387
http://purl.uniprot.org/uniprot/Q96CW1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19033387