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http://purl.uniprot.org/citations/27008177http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27008177http://www.w3.org/2000/01/rdf-schema#comment"Cullin-3 (CUL3)-based ubiquitin ligases regulate endosome maturation and trafficking of endocytic cargo to lysosomes in mammalian cells. Here, we report that these functions depend on SPOPL, a substrate-specific CUL3 adaptor. We find that SPOPL associates with endosomes and is required for both the formation of multivesicular bodies (MVBs) and the endocytic host cell entry of influenza A virus. In SPOPL-depleted cells, endosomes are enlarged and fail to acquire intraluminal vesicles (ILVs). We identify a critical substrate ubiquitinated by CUL3-SPOPL as EPS15, an endocytic adaptor that also associates with the ESCRT-0 complex members HRS and STAM on endosomes. Indeed, EPS15 is ubiquitinated in a SPOPL-dependent manner, and accumulates with HRS in cells lacking SPOPL. Together, our data indicates that a CUL3-SPOPL E3 ubiquitin ligase complex regulates endocytic trafficking and MVB formation by ubiquitinating and degrading EPS15 at endosomes, thereby influencing influenza A virus infection as well as degradation of EGFR and other EPS15 targets."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.org/dc/terms/identifier"doi:10.7554/elife.13841"xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Helenius A."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Greber U.F."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Peter M."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Yamauchi Y."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Barnes C.A."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Enchev R.I."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Stoffel-Studer I."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Ulbricht A."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Meyer-Schaller N."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Huotari J."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/author"Gschweitl M."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/pages"e13841"xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/title"A SPOPL/Cullin-3 ubiquitin ligase complex regulates endocytic trafficking by targeting EPS15 at endosomes."xsd:string
http://purl.uniprot.org/citations/27008177http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/27008177http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27008177
http://purl.uniprot.org/citations/27008177http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27008177
http://purl.uniprot.org/uniprot/#_B7Z240-mappedCitation-27008177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27008177
http://purl.uniprot.org/uniprot/#_B3KR37-mappedCitation-27008177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27008177
http://purl.uniprot.org/uniprot/#_B4DEY7-mappedCitation-27008177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27008177
http://purl.uniprot.org/uniprot/#_B7Z600-mappedCitation-27008177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27008177