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http://purl.uniprot.org/citations/23893131http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23893131http://www.w3.org/2000/01/rdf-schema#comment"The Arp2/3 complex mediates formation of complex cellular structures such as lamellipodia by nucleating branched actin filaments. Arp2/3-complex activity is precisely controlled by over a dozen regulators, yet the structural mechanism by which regulators interact with the complex is unknown. GMF is a recently discovered regulator of the Arp2/3 complex that can inhibit nucleation and disassemble branches. We solved the structure of the 240-kDa assembly of Mus musculus GMF and Bos taurus Arp2/3 complex and found that GMF binds the barbed end of Arp2, overlapping with the proposed binding site of WASP-family proteins. The structure suggests that GMF can bind branch junctions in the manner that cofilin binds filament sides, consistent with a modified cofilin-like mechanism for debranching by GMF. The GMF-Arp2 interface reveals how the ADF-H actin-binding domain in GMF is exploited to specifically recognize Arp2/3 complex and not actin."xsd:string
http://purl.uniprot.org/citations/23893131http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2628"xsd:string
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/author"Nolen B.J."xsd:string
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/author"Luan Q."xsd:string
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/pages"1062-1068"xsd:string
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/title"Structural basis for regulation of Arp2/3 complex by GMF."xsd:string
http://purl.uniprot.org/citations/23893131http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/23893131http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23893131
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