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http://purl.uniprot.org/citations/17609109http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17609109http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17609109http://www.w3.org/2000/01/rdf-schema#comment"Multiple modes of endocytosis require actin-dependent remodeling of the plasma membrane; however, neither the factors linking these processes nor their mechanisms of action are understood. The sorting nexin, SNX9, localizes to clathrin-coated pits where it interacts with dynamin and functions in clathrin-mediated endocytosis. Here, we demonstrate that SNX9 also localizes to actin-rich structures implicated in fluid-phase uptake, including tubular membranes containing GPI-anchored proteins and dorsal membrane ruffles. Moreover, we show that SNX9 is critical for dorsal ruffle formation and for clathrin-independent, actin-dependent fluid-phase endocytosis. In vitro, SNX9 directly associates with N-WASP, an Arp2/3 complex activator, and stimulates N-WASP/Arp2/3-mediated actin assembly. SNX9-stimulated actin polymerization is greatly enhanced by PI(4,5)P(2)-containing liposomes, due in part to PI(4,5)P(2)-induced SNX9 oligomerization. These results suggest a mechanism for the spatial and temporal regulation of N-WASP-dependent actin assembly and implicate SNX9 in directly coupling actin dynamics to membrane remodeling during multiple modes of endocytosis."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2007.04.014"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2007.04.014"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/author"Schmid S.L."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/author"Schmid S.L."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/author"Waterman-Storer C.M."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/author"Waterman-Storer C.M."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/author"Yarar D."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/author"Yarar D."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/pages"43-56"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/pages"43-56"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/title"SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/title"SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis."xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/17609109http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/17609109http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17609109
http://purl.uniprot.org/citations/17609109http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17609109
http://purl.uniprot.org/citations/17609109http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17609109
http://purl.uniprot.org/citations/17609109http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17609109