| First Author | Da Cruz S | Year | 2008 |
| Journal | Biochim Biophys Acta | Volume | 1783 |
| Issue | 5 | Pages | 904-11 |
| PubMed ID | 18339324 | Mgi Jnum | J:136807 |
| Mgi Id | MGI:3797153 | Doi | 10.1016/j.bbamcr.2008.02.006 |
| Citation | Da Cruz S, et al. (2008) SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability. Biochim Biophys Acta 1783(5):904-11 |
| abstractText | 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. |
