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http://purl.uniprot.org/citations/23382462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23382462http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23382462http://www.w3.org/2000/01/rdf-schema#comment"Eukaryotic cells critically depend on the correct regulation of intracellular vesicular trafficking to transport biological material. The Rab subfamily of small guanosine triphosphatases controls these processes by acting as a molecular on/off switch. To fulfill their function, active Rab proteins need to localize to intracellular membranes via posttranslationally attached geranylgeranyl lipids. Each member of the manifold Rab family localizes specifically to a distinct membrane, but it is unclear how this specific membrane recruitment is achieved. Here, we demonstrate that Rab-activating guanosine diphosphate/guanosine triphosphate exchange factors (GEFs) display the minimal targeting machinery for recruiting Rabs from the cytosol to the correct membrane using the Rab-GEF pairs Rab5A-Rabex-5, Rab1A-DrrA, and Rab8-Rabin8 as model systems. Specific mistargeting of Rabex-5/DrrA/Rabin8 to mitochondria led to catalytic recruitment of Rab5A/Rab1A/Rab8A in a time-dependent manner that required the catalytic activity of the GEF. Therefore, RabGEFs are major determinants for specific Rab membrane targeting."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201209113"xsd:string
http://purl.uniprot.org/citations/23382462http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201209113"xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Goody R.S."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Goody R.S."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Itzen A."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Itzen A."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Wu Y.W."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Wu Y.W."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Rey J."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Rey J."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Bastiaens P."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Bastiaens P."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Bluemer J."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Bluemer J."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Dehmelt L."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Dehmelt L."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Mazel T."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/author"Mazel T."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/23382462http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string