SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability. - Archive ouverte HAL
Article Dans Une Revue BBA - Biochimica et Biophysica Acta Année : 2008

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

Résumé

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.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.
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Dates et versions

hal-00315185 , version 1 (27-08-2008)

Identifiants

  • HAL Id : hal-00315185 , version 1
  • PUBMED : 18339324

Citer

S. Dacruz, Pa Parone, P. Gonzalo, Wv Bienvenut, D. Tondera, et al.. SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability.. BBA - Biochimica et Biophysica Acta, 2008, xxx, pp.904-911. ⟨hal-00315185⟩
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