%0 Journal Article %1 lorenziMitochondrialTMEM177Associates2018 %A Lorenzi, Isotta %A Oeljeklaus, Silke %A Aich, Abhishek %A Ronsör, Christin %A Callegari, Sylvie %A Dudek, Jan %A Warscheid, Bettina %A Dennerlein, Sven %A Rehling, Peter %C Netherlands %D 2018 %J Biochimica et biophysica acta. Molecular cell research %K COX Cells,Humans,Membrane Complex IV/genetics/*metabolism,HEK293 Membranes/*metabolism,Mitochondrial Proteins/genetics/*metabolism,Mitochondria,Mitochondrial Proteins/genetics/*metabolism,Oxidative Transport assembly,COX2 biogenesis,COX20 chain,to_read chaperone,Electron phosphorylation,Respiratory %N 2 %P 323--333 %R 10.1016/j.bbamcr.2017.11.010 %T The Mitochondrial TMEM177 Associates with COX20 during COX2 Biogenesis. %V 1865 %X 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(A)-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(A)-site formation.

@article{lorenziMitochondrialTMEM177Associates2018, 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(A)-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(A)-site formation.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {Netherlands}, author = {Lorenzi, Isotta and Oeljeklaus, Silke and Aich, Abhishek and Rons{\"o}r, Christin and Callegari, Sylvie and Dudek, Jan and Warscheid, Bettina and Dennerlein, Sven and Rehling, Peter}, biburl = {https://www.bibsonomy.org/bibtex/2d031ffa5d725333a04aeeb47c5803454/warscheidlab}, copyright = {Copyright {\copyright} 2017 The Authors. Published by Elsevier B.V. All rights reserved.}, doi = {10.1016/j.bbamcr.2017.11.010}, interhash = {03e68c2a300bcc01c8c5b5cdd0cc53f8}, intrahash = {d031ffa5d725333a04aeeb47c5803454}, issn = {0167-4889 1878-2434}, journal = {Biochimica et biophysica acta. Molecular cell research}, keywords = {COX Cells,Humans,Membrane Complex IV/genetics/*metabolism,HEK293 Membranes/*metabolism,Mitochondrial Proteins/genetics/*metabolism,Mitochondria,Mitochondrial Proteins/genetics/*metabolism,Oxidative Transport assembly,COX2 biogenesis,COX20 chain,to_read chaperone,Electron phosphorylation,Respiratory}, langid = {english}, month = feb, number = 2, pages = {323--333}, pmcid = {PMC5764226}, pmid = {29154948}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {The Mitochondrial {{TMEM177}} Associates with {{COX20}} during {{COX2}} Biogenesis.}, volume = 1865, year = 2018 }