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  The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.

Lorenzi, I., Oeljeklaus, S., Aich, A., Ronsör, C., Callegari, S., Dudek, J., et al. (2018). The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis. Biochimica et Biophysica Acta - Molecular Cell Research, 1865(2), 323-333. doi:10.1016/j.bbamcr.2017.11.010.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-37BA-A Version Permalink: http://hdl.handle.net/21.11116/0000-0003-8816-B
Genre: Journal Article

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 Creators:
Lorenzi, I., Author
Oeljeklaus, S., Author
Aich, A., Author
Ronsör, C., Author
Callegari, S., Author
Dudek, J., Author
Warscheid, B., Author
Dennerlein, S., Author
Rehling, P.1, Author              
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: COX assembly; COX2 biogenesis; COX20 chaperone; Mitochondria; Oxidative phosphorylation; Respiratory chain
 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.

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Language(s): eng - English
 Dates: 2017-11-152018-02
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bbamcr.2017.11.010
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Title: Biochimica et Biophysica Acta - Molecular Cell Research
Source Genre: Journal
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Pages: - Volume / Issue: 1865 (2) Sequence Number: - Start / End Page: 323 - 333 Identifier: -