RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/29030480http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29030480http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29030480http://www.w3.org/2000/01/rdf-schema#comment"Epidermal growth factor (EGF) activates the EGF receptor (EGFR) and stimulates its internalization and trafficking to lysosomes for degradation. However, a percentage of EGFR undergoes ligand-independent endocytosis and is rapidly recycled back to the plasma membrane. Importantly, alterations in EGFR recycling are a common hallmark of cancer, and yet, our understanding of the machineries controlling the fate of endocytosed EGFR is incomplete. Intersectin-s is a multi-domain adaptor protein that is required for internalization of EGFR Here, we discover that intersectin-s binds DENND2B, a guanine nucleotide exchange factor for the exocytic GTPase Rab13, and this interaction promotes recycling of ligand-free EGFR to the cell surface. Intriguingly, upon EGF treatment, DENND2B is phosphorylated by protein kinase D and dissociates from intersectin-s, allowing for receptor targeting to degradation. Our study thus reveals a novel mechanism controlling the fate of internalized EGFR with important implications for cancer."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.org/dc/terms/identifier"doi:10.15252/embr.201744034"xsd:string
http://purl.uniprot.org/citations/29030480http://purl.org/dc/terms/identifier"doi:10.15252/embr.201744034"xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Han C."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Han C."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Ioannou M.S."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Ioannou M.S."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Kulasekaran G."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Kulasekaran G."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"McPherson P.S."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"McPherson P.S."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Nossova N."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Nossova N."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Han T."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Han T."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Tse S."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Tse S."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Fotouhi M."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Fotouhi M."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Mannard E."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Mannard E."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Morein J.J."xsd:string
http://purl.uniprot.org/citations/29030480http://purl.uniprot.org/core/author"Morein J.J."xsd:string