RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17438143http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17438143http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17438143http://www.w3.org/2000/01/rdf-schema#comment"S100A1, a Ca(2+)-sensing protein of the EF-hand family that is expressed predominantly in cardiac muscle, plays a pivotal role in cardiac contractility in vitro and in vivo. It has recently been demonstrated that by restoring Ca(2+) homeostasis, S100A1 was able to rescue contractile dysfunction in failing rat hearts. Myocardial contractility is regulated not only by Ca(2+) homeostasis but also by energy metabolism, in particular the production of ATP. Here, we report a novel interaction of S100A1 with mitochondrial F(1)-ATPase, which affects F(1)-ATPase activity and cellular ATP production. In particular, cardiomyocytes that overexpress S100A1 exhibited a higher ATP content than control cells, whereas knockdown of S100A1 expression decreased ATP levels. In pull-down experiments, we identified the alpha- and beta-chain of F(1)-ATPase to interact with S100A1 in a Ca(2+)-dependent manner. The interaction was confirmed by colocalization studies of S100A1 and F(1)-ATPase and the analysis of the S100A1-F(1)-ATPase complex by gel filtration chromatography. The functional impact of this association is highlighted by an S100A1-mediated increase of F(1)-ATPase activity. Consistently, ATP synthase activity is reduced in cardiomyocytes from S100A1 knockout mice. Our data indicate that S100A1 might play a key role in cardiac energy metabolism."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.org/dc/terms/identifier"doi:10.1128/mcb.02045-06"xsd:string
http://purl.uniprot.org/citations/17438143http://purl.org/dc/terms/identifier"doi:10.1128/mcb.02045-06"xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Aebi U."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Aebi U."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Walker J.E."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Walker J.E."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Katus H.A."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Katus H.A."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Koch W.J."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Koch W.J."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Gledhill J.R."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Gledhill J.R."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Boerries M."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Boerries M."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Most P."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Most P."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Schoenenberger C.A."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/author"Schoenenberger C.A."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/17438143http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string