| http://purl.uniprot.org/citations/24898248 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24898248 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24898248 | http://www.w3.org/2000/01/rdf-schema#comment | "Mitochondria capture and subsequently release Ca(2+) ions, thereby sensing and shaping cellular Ca(2+) signals. The Ca(2+) uniporter MCU mediates Ca(2+) uptake, whereas NCLX (mitochondrial Na/Ca exchanger) and LETM1 (leucine zipper-EF-hand-containing transmembrane protein 1) were proposed to exchange Ca(2+) against Na(+) or H(+), respectively. Here we study the role of these ion exchangers in mitochondrial Ca(2+) extrusion and in Ca(2+)-metabolic coupling. Both NCLX and LETM1 proteins were expressed in HeLa cells mitochondria. The rate of mitochondrial Ca(2+) efflux, measured with a genetically encoded indicator during agonist stimulations, increased with the amplitude of mitochondrial Ca(2+) ([Ca(2+)]mt) elevations. NCLX overexpression enhanced the rates of Ca(2+) efflux, whereas increasing LETM1 levels had no impact on Ca(2+) extrusion. The fluorescence of the redox-sensitive probe roGFP increased during [Ca(2+)]mt elevations, indicating a net reduction of the matrix. This redox response was abolished by NCLX overexpression and restored by the Na(+)/Ca(2+) exchanger inhibitor CGP37157. The [Ca(2+)]mt elevations were associated with increases in the autofluorescence of NAD(P)H, whose amplitude was strongly reduced by NCLX overexpression, an effect reverted by Na(+)/Ca(2+) exchange inhibition. We conclude that NCLX, but not LETM1, mediates Ca(2+) extrusion from mitochondria. By controlling the duration of matrix Ca(2+) elevations, NCLX contributes to the regulation of NAD(P)H production and to the conversion of Ca(2+) signals into redox changes."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.540898"xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.540898"xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Demaurex N."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Demaurex N."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Sekler I."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Sekler I."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Wiederkehr A."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Wiederkehr A."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Castelbou C."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Castelbou C."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "De Marchi U."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "De Marchi U."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Santo-Domingo J."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/author | "Santo-Domingo J."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/pages | "20377-20385"xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/pages | "20377-20385"xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/title | "NCLX protein, but not LETM1, mediates mitochondrial Ca2+ extrusion, thereby limiting Ca2+-induced NAD(P)H production and modulating matrix redox state."xsd:string |
| http://purl.uniprot.org/citations/24898248 | http://purl.uniprot.org/core/title | "NCLX protein, but not LETM1, mediates mitochondrial Ca2+ extrusion, thereby limiting Ca2+-induced NAD(P)H production and modulating matrix redox state."xsd:string |