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http://purl.uniprot.org/citations/28775156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28775156http://www.w3.org/2000/01/rdf-schema#comment"Sharpin, a multifunctional adaptor protein, regulates several signalling pathways. For example, Sharpin enhances signal-induced NF-κB signalling as part of the linear ubiquitin assembly complex (LUBAC) and inhibits integrins, the T cell receptor, caspase 1 and PTEN. However, despite recent insights into Sharpin and LUBAC function, a systematic approach to identify the signalling pathways regulated by Sharpin has not been reported. Here, we present the first 'Sharpin interactome', which identifies a large number of novel potential Sharpin interactors in addition to several known ones. These data suggest that Sharpin and LUBAC might regulate a larger number of biological processes than previously identified, such as endosomal trafficking, RNA processing, metabolism and cytoskeleton regulation. Importantly, using the Sharpin interactome, we have identified a novel role for Sharpin in lamellipodium formation. We demonstrate that Sharpin interacts with Arp2/3, a protein complex that catalyses actin filament branching. We have identified the Arp2/3-binding site in Sharpin and demonstrate using a specific Arp2/3-binding deficient mutant that the Sharpin-Arp2/3 interaction promotes lamellipodium formation in a LUBAC-independent fashion.This article has an associated First Person interview with the first author of the paper."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.org/dc/terms/identifier"doi:10.1242/jcs.200329"xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Lappalainen P."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Deguchi T."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Pouwels J."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Khan M.H."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Humphries M.J."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Kremneva E."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Jacquemet G."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Butt U."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Miihkinen M."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/author"Salomaa S.I."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/pages"3094-3107"xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/title"The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex."xsd:string
http://purl.uniprot.org/citations/28775156http://purl.uniprot.org/core/volume"130"xsd:string
http://purl.uniprot.org/citations/28775156http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28775156
http://purl.uniprot.org/citations/28775156http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28775156
http://purl.uniprot.org/uniprot/#_Q9H0F6-mappedCitation-28775156http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28775156
http://purl.uniprot.org/uniprot/#_Q6PJD5-mappedCitation-28775156http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28775156
http://purl.uniprot.org/uniprot/Q9H0F6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28775156
http://purl.uniprot.org/uniprot/Q6PJD5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28775156