<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Da Cruz S</dc:creator>
  <dc:creator>Parone PA</dc:creator>
  <dc:creator>Gonzalo P</dc:creator>
  <dc:creator>Bienvenut WV</dc:creator>
  <dc:creator>Tondera D</dc:creator>
  <dc:creator>Jourdain A</dc:creator>
  <dc:creator>Quadroni M</dc:creator>
  <dc:creator>Martinou JC</dc:creator>
  <dc:date>2008</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">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.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/220138</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamcr.2008.02.006</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/18339324</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Biochimica et biophysica acta. - 2008</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Blood Proteins</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Cells, Cultured</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Electron Transport Complex I</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Electron Transport Complex IV</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">HeLa Cells</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Immunoprecipitation</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Membrane Proteins</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Mitochondria</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Mitochondrial Membranes</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Mitochondrial Proteins</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Repressor Proteins</dc:subject>
  <dc:title xmlns:ns14="xml" ns14:lang="en">SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
