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| http://purl.uniprot.org/citations/25088759 | http://www.w3.org/2000/01/rdf-schema#comment | "The major cardiac voltage-gated sodium channel Nav1.5 associates with proteins that regulate its biosynthesis, localization, activity and degradation. Identification of partner proteins is crucial for a better understanding of the channel regulation. Using a yeast two-hybrid screen, we identified dynamitin as a Nav1.5-interacting protein. Dynamitin is part of the microtubule-binding multiprotein complex dynactin. When overexpressed it is a potent inhibitor of dynein/kinesin-mediated transport along the microtubules by disrupting the dynactin complex and dissociating cargoes from microtubules. The use of deletion constructs showed that the C-terminal domain of dynamitin is essential for binding to the first intracellular interdomain of Nav1.5. Co-immunoprecipitation assays confirmed the association between Nav1.5 and dynamitin in mouse heart extracts. Immunostaining experiments showed that dynamitin and Nav1.5 co-localize at intercalated discs of mouse cardiomyocytes. The whole-cell patch-clamp technique was applied to test the functional link between Nav1.5 and dynamitin. Dynamitin overexpression in HEK-293 (human embryonic kidney 293) cells expressing Nav1.5 resulted in a decrease in sodium current density in the membrane with no modification of the channel-gating properties. Biotinylation experiments produced similar information with a reduction in Nav1.5 at the cell surface when dynactin-dependent transport was inhibited. The present study strongly suggests that dynamitin is involved in the regulation of Nav1.5 cell-surface density."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20140604"xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/author | "Le Bouffant F."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/author | "Allouis M."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/author | "Chatin B."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/author | "Colombier P."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/author | "Gamblin A.L."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/pages | "339-349"xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/title | "Dynamitin affects cell-surface expression of voltage-gated sodium channel Nav1.5."xsd:string |
| http://purl.uniprot.org/citations/25088759 | http://purl.uniprot.org/core/volume | "463"xsd:string |
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