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http://purl.uniprot.org/citations/21693584http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21693584http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21693584http://www.w3.org/2000/01/rdf-schema#comment"The Rac1 GTPase controls cytoskeletal dynamics and is a key regulator of cell spreading and migration mediated by signaling through effector proteins, such as the PAK kinases and the Scar and WAVE proteins. We previously identified a series of regulatory proteins that associate with Rac1 through its hypervariable C-terminal domain, including the Rac1 activator β-Pix (also known as Rho guanine-nucleotide-exchange factor 7) and the membrane adapter caveolin-1. Here, we show that Rac1 associates, through its C-terminus, with the F-BAR domain protein PACSIN2, an inducer of membrane tubulation and a regulator of endocytosis. We show that Rac1 localizes with PACSIN2 at intracellular tubular structures and on early endosomes. Active Rac1 induces a loss of PACSIN2-positive tubular structures. By contrast, Rac1 inhibition results in an accumulation of PACSIN2-positive tubules. In addition, PACSIN2 appears to regulate Rac1 signaling; siRNA-mediated loss of PACSIN2 increases the levels of Rac1-GTP and promotes cell spreading and migration in a wound healing assay. Moreover, ectopic expression of PACSIN2 reduces Rac1-GTP levels in a fashion that is dependent on the PACSIN2-Rac1 interaction, on the membrane-tubulating capacity of PACSIN2 and on dynamin. These data identify the BAR-domain protein PACSIN2 as a Rac1 interactor that regulates Rac1-mediated cell spreading and migration."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.org/dc/terms/identifier"doi:10.1242/jcs.080630"xsd:string
http://purl.uniprot.org/citations/21693584http://purl.org/dc/terms/identifier"doi:10.1242/jcs.080630"xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Hordijk P.L."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Hordijk P.L."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Deelder A.M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Deelder A.M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Hensbergen P.J."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Hensbergen P.J."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Plomann M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Plomann M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Anthony E.C."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Anthony E.C."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Fernandez-Borja M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Fernandez-Borja M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"de Kreuk B.J."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"de Kreuk B.J."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Nethe M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/author"Nethe M."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/21693584http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string