RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/20406883http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20406883http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20406883http://www.w3.org/2000/01/rdf-schema#comment"Dictyostelium and human MidA are homologous proteins that belong to a family of proteins of unknown function called DUF185. Using yeast two-hybrid screening and pull-down experiments, we showed that both proteins interact with the mitochondrial complex I subunit NDUFS2. Consistent with this, Dictyostelium cells lacking MidA showed a specific defect in complex I activity, and knockdown of human MidA in HEK293T cells resulted in reduced levels of assembled complex I. These results indicate a role for MidA in complex I assembly or stability. A structural bioinformatics analysis suggested the presence of a methyltransferase domain; this was further supported by site-directed mutagenesis of specific residues from the putative catalytic site. Interestingly, this complex I deficiency in a Dictyostelium midA(-) mutant causes a complex phenotypic outcome, which includes phototaxis and thermotaxis defects. We found that these aspects of the phenotype are mediated by a chronic activation of AMPK, revealing a possible role of AMPK signaling in complex I cytopathology."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.org/dc/terms/identifier"doi:10.1242/jcs.066076"xsd:string
http://purl.uniprot.org/citations/20406883http://purl.org/dc/terms/identifier"doi:10.1242/jcs.066076"xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Calvo-Garrido J."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Calvo-Garrido J."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Carilla-Latorre S."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Carilla-Latorre S."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Escalante R."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Escalante R."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Fisher P.R."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Fisher P.R."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Valencia A."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Valencia A."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Annesley S.J."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Annesley S.J."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Accari S.L."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Accari S.L."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Gallardo M.E."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Gallardo M.E."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Garesse R."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Garesse R."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Grana O."xsd:string
http://purl.uniprot.org/citations/20406883http://purl.uniprot.org/core/author"Grana O."xsd:string