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| http://purl.uniprot.org/citations/17637832 | http://www.w3.org/2000/01/rdf-schema#comment | "Rab3a is a small GTPase that binds selectively to secretory vesicles and switches between active, GTP-bound and inactive, GDP-bound conformations. In yeast, Rab and SM-genes interact genetically to promote vesicle targeting/fusion. We tested different Rab3a conformations and genetic interactions with the SM-gene munc18-1 on the docking function of Rab3a in mammalian chromaffin cells. We expressed Rab3a mutants locked in the GTP- or GDP-bound form in wild-type and munc18-1 null mutant cells and analyzed secretory vesicle distribution. We confirmed that wild-type Rab3a promotes vesicle docking in wild-type cells. Unexpectedly, both GTP- and GDP-locked Rab3a mutants did not promote docking. Furthermore, wild-type Rab3a did not promote docking in munc18-1 null cells and GTP- and GDP-Rab3a both decreased the amount of docked vesicles. The results show that GTP- and GDP-locked conformations do not support a Munc18-1 dependent role of Rab3a in docking. This suggests that nucleotide cycling is required to support docking and that this action of Rab3a is upstream of Munc18-1."xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0000616"xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/author | "Toonen R.F."xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/author | "Verhage M."xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/author | "van Weering J.R."xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/pages | "e616"xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/title | "The role of Rab3a in secretory vesicle docking requires association/dissociation of guanidine phosphates and Munc18-1."xsd:string |
| http://purl.uniprot.org/citations/17637832 | http://purl.uniprot.org/core/volume | "2"xsd:string |
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