| http://purl.uniprot.org/citations/23836888 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23836888 | http://www.w3.org/2000/01/rdf-schema#comment | "Voltage-gated sodium channel (NaV) trafficking is incompletely understood. Post-translational modifications of NaVs and/or auxiliary subunits and protein-protein interactions have been posited as NaV-trafficking mechanisms. Here, we tested if modification of the axonal collapsin response mediator protein 2 (CRMP2) by a small ubiquitin-like modifier (SUMO) could affect NaV trafficking; CRMP2 alters the extent of NaV slow inactivation conferred by the anti-epileptic (R)-lacosamide, implying NaV-CRMP2 functional coupling. Expression of a CRMP2 SUMOylation-incompetent mutant (CRMP2-K374A) in neuronal model catecholamine A differentiated (CAD) cells did not alter lacosamide-induced NaV slow inactivation compared with CAD cells expressing wild type CRMP2. Like wild type CRMP2, CRMP2-K374A expressed robustly in CAD cells. Neurite outgrowth, a canonical CRMP2 function, was moderately reduced by the mutation but was still significantly higher than enhanced GFP-transfected cortical neurons. Notably, huwentoxin-IV-sensitive NaV1.7 currents, which predominate in CAD cells, were significantly reduced in CAD cells expressing CRMP2-K374A. Increasing deSUMOylation with sentrin/SUMO-specific protease SENP1 or SENP2 in wild type CRMP2-expressing CAD cells decreased NaV1.7 currents. Consistent with a reduction in current density, biotinylation revealed a significant reduction in surface NaV1.7 levels in CAD cells expressing CRMP2-K374A; surface NaV1.7 expression was also decreased by SENP1 + SENP2 overexpression. Currents in HEK293 cells stably expressing NaV1.7 were reduced by CRMP2-K374A in a manner dependent on the E2-conjugating enzyme Ubc9. No decrement in current density was observed in HEK293 cells co-expressing CRMP2-K374A and NaV1.1 or NaV1.3. Diminution of sodium currents, largely NaV1.7, was recapitulated in sensory neurons expressing CRMP2-K374A. Our study elucidates a novel regulatory mechanism that utilizes CRMP2 SUMOylation to choreograph NaV1.7 trafficking."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.474924"xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/author | "Khanna R."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/author | "Xiao Y."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/author | "Wilson S.M."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/author | "Ju W."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/author | "Dustrude E.T."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/pages | "24316-24331"xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/title | "CRMP2 protein SUMOylation modulates NaV1.7 channel trafficking."xsd:string |
| http://purl.uniprot.org/citations/23836888 | http://purl.uniprot.org/core/volume | "288"xsd:string |
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| http://purl.uniprot.org/uniprot/#_B1AYL0-mappedCitation-23836888 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23836888 |
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