The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis |
| |
| Authors: | Isotta Lorenzi Silke Oeljeklaus Abhishek Aich Christin Ronsör Sylvie Callegari Jan Dudek Bettina Warscheid Sven Dennerlein Peter Rehling |
| |
| Institution: | 1. Department of Cellular Biochemistry, University Medical Centre Göttingen, GZMB, D-37073 Göttingen, Germany;2. Faculty of Biology, Department of Biochemistry and Functional Proteomics, University Freiburg, D-79104 Freiburg, Germany;3. BIOSS Centre for Biological Signalling Studies, University of Freiburg, D-79104 Freiburg, Germany;4. Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany |
| |
| Abstract: | The three mitochondrial-encoded proteins, COX1, COX2, and COX3, form the core of the cytochrome c oxidase. Upon synthesis, COX2 engages with COX20 in the inner mitochondrial membrane, a scaffold protein that recruits metallochaperones for copper delivery to the CuA-Site of COX2. Here we identified the human protein, TMEM177 as a constituent of the COX20 interaction network. Loss or increase in the amount of TMEM177 affects COX20 abundance leading to reduced or increased COX20 levels respectively. TMEM177 associates with newly synthesized COX2 and SCO2 in a COX20-dependent manner. Our data shows that by unbalancing the amount of TMEM177, newly synthesized COX2 accumulates in a COX20-associated state. We conclude that TMEM177 promotes assembly of COX2 at the level of CuA-site formation. |
| |
| Keywords: | COX2 biogenesis COX assembly COX20 chaperone Mitochondria Oxidative phosphorylation Respiratory chain |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
