SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability

Article Article scientifique Article SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability eng 2008 author Da Cruz Sandrine 528962 author Parone Philippe 528921 author Gonzalo Philippe 639740 author Bienvenut Willy V. author Tondera Daniel 629037 author Jourdain Alexis 563333 author Quadroni Manfredo author Martinou Jean-Claude 27293 904-911 10.1016/j.bbamcr.2008.02.006 18339324 0006-3002 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. Dewey 570 46 Département de biologie cellulaire 165 false Biochimica et biophysica acta 1783 38239319-8d74-439a-9e5c-713493c725f1 Article (Published version) Public file1.pdf 638170 application/pdf openAccess Faculté des sciences / Section de biologie / Département de biologie cellulaire

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SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability	Biochimica et biophysica acta			2008	685	694

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Gonzalo, Philippe