AI Article Synopsis
- The three mitochondrial proteins COX1, COX2, and COX3 are essential for forming cytochrome c oxidase, with COX2 interacting with the scaffold protein COX20 for copper delivery.
- TMEM177 is identified as part of the COX20 network, influencing the levels of COX20; too little or too much TMEM177 alters COX20 abundance.
- The study concludes that TMEM177 plays a key role in assembling COX2 during the formation of its copper site by interacting with newly synthesized COX2 and SCO2 in a COX20-dependent manner.
Article 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 Cu-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 Cu-site formation.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5764226 | PMC |
| http://dx.doi.org/10.1016/j.bbamcr.2017.11.010 | DOI Listing |
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The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.
Biochim Biophys Acta Mol Cell Res
February 2018
Department of Cellular Biochemistry, University Medical Centre Göttingen, GZMB, D-37073 Göttingen, Germany; Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany. Electronic address:
Article Synopsis
- The three mitochondrial proteins COX1, COX2, and COX3 are essential for forming cytochrome c oxidase, with COX2 interacting with the scaffold protein COX20 for copper delivery.
- TMEM177 is identified as part of the COX20 network, influencing the levels of COX20; too little or too much TMEM177 alters COX20 abundance.
- The study concludes that TMEM177 plays a key role in assembling COX2 during the formation of its copper site by interacting with newly synthesized COX2 and SCO2 in a COX20-dependent manner.
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