1. The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis
- Author
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Silke Oeljeklaus, Sven Dennerlein, Bettina Warscheid, Jan Dudek, Isotta Lorenzi, Peter Rehling, Abhishek Aich, Christin Ronsör, and Sylvie Callegari
- Subjects
0301 basic medicine ,Scaffold protein ,Respiratory chain ,macromolecular substances ,Mitochondrion ,Biology ,COX assembly ,COX20 chaperone ,Article ,Electron Transport Complex IV ,Mitochondrial Proteins ,Metallochaperones ,03 medical and health sciences ,0302 clinical medicine ,Humans ,Cytochrome c oxidase ,Oxidative phosphorylation ,Inner mitochondrial membrane ,Molecular Biology ,Membrane Proteins ,food and beverages ,Cell Biology ,Mitochondria ,Cell biology ,HEK293 Cells ,030104 developmental biology ,Membrane protein ,Mitochondrial Membranes ,biology.protein ,COX2 biogenesis ,030217 neurology & neurosurgery - 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., Highlights • TMEM177 is a mitochondrial inner membrane protein. • COX20 associates with TMEM177. • The TMEM177 protein forms a complex with COX2 and copper chaperones.
- Published
- 2018