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http://purl.uniprot.org/citations/18339324http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18339324http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18339324http://www.w3.org/2000/01/rdf-schema#comment"Stomatin is a member of a large family of proteins including prohibitins, HflK/C, flotillins, mechanoreceptors and plant defense proteins, that are thought to play a role in protein turnover. Using different proteomic approaches, we and others have identified SLP-2, a member of the stomatin gene family, as a component of the mitochondria. In this study, we show that SLP-2 is strongly associated with the mitochondrial inner membrane and that it interacts with prohibitins. Depleting HeLa cells of SLP-2 lead to increased proteolysis of prohibitins and of subunits of the respiratory chain complexes I and IV. Further supporting the role of SLP-2 in regulating the stability of specific mitochondrial proteins, we found that SLP-2 is up-regulated under conditions of mitochondrial stress leading to increased protein turnover. These data indicate that SLP-2 plays a role in regulating the stability of mitochondrial proteins including prohibitins and subunits of respiratory chain complexes."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.org/dc/terms/identifier"doi:10.1016/j.bbamcr.2008.02.006"xsd:string
http://purl.uniprot.org/citations/18339324http://purl.org/dc/terms/identifier"doi:10.1016/j.bbamcr.2008.02.006"xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Bienvenut W.V."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Bienvenut W.V."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Quadroni M."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Quadroni M."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Jourdain A."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Jourdain A."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Martinou J.C."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Martinou J.C."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Da Cruz S."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Da Cruz S."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Parone P.A."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Parone P.A."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Tondera D."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Tondera D."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Gonzalo P."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/author"Gonzalo P."xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/18339324http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string