UNIGE document Scientific Article
previous document  unige:18  next document
add to browser collection
Title

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

Authors
Bienvenut, Willy V.
Quadroni, Manfredo
Published in Biochimica et Biophysica Acta. 2008, vol. 1783, p. 904-911
Abstract 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.
Identifiers
PMID: 18339324
Full text
Structures
Citation
(ISO format)
DA CRUZ, Sandrine et al. SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability. In: Biochimica et Biophysica Acta, 2008, vol. 1783, p. 904-911. https://archive-ouverte.unige.ch/unige:18

196 hits

190 downloads

Update

Deposited on : 2008-10-29

Export document
Format :
Citation style :