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http://purl.uniprot.org/citations/26774128http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26774128http://www.w3.org/2000/01/rdf-schema#comment"Arpin is a newly discovered regulator of actin polymerization at the cell leading edge, which steers cell migration by exerting a negative control on the Arp2/3 complex. Arpin proteins have an acidic tail homologous to the acidic motif of the VCA domain of nucleation-promoting factors (NPFs). This tail is predicted to compete with the VCA of NPFs for binding to the Arp2/3 complex, thereby mitigating activation and/or tethering of the complex to sites of actin branching. Here, we investigated the structure of full-length Arpin using synchrotron small-angle X-ray scattering, and of its acidic tail in complex with an ankyrin repeats domain using X-ray crystallography. The data were combined in a hybrid model in which the acidic tail extends from the globular core as a linear peptide and forms a primary epitope that is readily accessible in unbound Arpin and suffices to tether Arpin to interacting proteins with high affinity."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2015.12.001"xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Campanacci V."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Perez J."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Cherfils J."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Dang I."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Fetics S."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Gautreau A."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Aumont-Nicaise M."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/author"Thureau A."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/pages"252-260"xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/title"Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope."xsd:string
http://purl.uniprot.org/citations/26774128http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/26774128http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26774128
http://purl.uniprot.org/citations/26774128http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26774128
http://purl.uniprot.org/uniprot/#_H0YMP5-mappedCitation-26774128http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26774128
http://purl.uniprot.org/uniprot/#_Q7Z6K5-mappedCitation-26774128http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26774128
http://purl.uniprot.org/uniprot/#_Q9H2K2-mappedCitation-26774128http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26774128
http://purl.uniprot.org/uniprot/Q7Z6K5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/26774128
http://purl.uniprot.org/uniprot/Q9H2K2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/26774128
http://purl.uniprot.org/uniprot/H0YMP5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/26774128