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http://purl.uniprot.org/citations/24970086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24970086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24970086http://www.w3.org/2000/01/rdf-schema#comment"Dynamin superfamily molecular motors use guanosine triphosphate (GTP) as a source of energy for membrane-remodeling events. We found that knockdown of nucleoside diphosphate kinases (NDPKs) NM23-H1/H2, which produce GTP through adenosine triphosphate (ATP)-driven conversion of guanosine diphosphate (GDP), inhibited dynamin-mediated endocytosis. NM23-H1/H2 localized at clathrin-coated pits and interacted with the proline-rich domain of dynamin. In vitro, NM23-H1/H2 were recruited to dynamin-induced tubules, stimulated GTP-loading on dynamin, and triggered fission in the presence of ATP and GDP. NM23-H4, a mitochondria-specific NDPK, colocalized with mitochondrial dynamin-like OPA1 involved in mitochondria inner membrane fusion and increased GTP-loading on OPA1. Like OPA1 loss of function, silencing of NM23-H4 but not NM23-H1/H2 resulted in mitochondrial fragmentation, reflecting fusion defects. Thus, NDPKs interact with and provide GTP to dynamins, allowing these motor proteins to work with high thermodynamic efficiency."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.org/dc/terms/identifier"doi:10.1126/science.1253768"xsd:string
http://purl.uniprot.org/citations/24970086http://purl.org/dc/terms/identifier"doi:10.1126/science.1253768"xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Shen Q."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Shen Q."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Schlattner U."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Schlattner U."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Lacombe M.L."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Lacombe M.L."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Lascu I."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Lascu I."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Raposo G."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Raposo G."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Roux A."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Roux A."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Chavrier P."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Chavrier P."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Montagnac G."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Montagnac G."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Polo S."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"Polo S."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"van der Bliek A.M."xsd:string
http://purl.uniprot.org/citations/24970086http://purl.uniprot.org/core/author"van der Bliek A.M."xsd:string