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  Identification of TMEM126A as OXA1L-interacting protein reveals cotranslational quality control in mitochondria

Poerschke, S., Oeljeklaus, S., Cruz-Zaragoza, L., Schenzielorz, A., Dahal, D., Hillen, H. S., et al. (2024). Identification of TMEM126A as OXA1L-interacting protein reveals cotranslational quality control in mitochondria. Molecular Cell, 84(2), 345-358.e5. doi:10.1016/j.molcel.2023.12.013.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000E-5D17-1 Version Permalink: https://hdl.handle.net/21.11116/0000-000E-5D18-0
Genre: Journal Article

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1-s2.0-S1097276523010316-main.pdf (Publisher version), 6MB
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Version of Record 18 January 2024.
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Poerschke, S., Author
Oeljeklaus, S., Author
Cruz-Zaragoza, L.D., Author
Schenzielorz, A., Author
Dahal, D., Author
Hillen, H. S.1, Author           
Das, H., Author
Kremer, L.S., Author
Valpadashi, A., Author
Breuer, M., Author
Sattmann, J., Author
Richter-Dennerlein, R., Author
Warscheid, B., Author
Dennerlein, S., Author
Rehling, P.2, Author           
Affiliations:
1Research Group Structure and Function of Molecular Machines, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350269              
2MPI-NAT Fellow Mitochondrial Biogenesis and Assembly of membrane Protein Complexes, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3505610              

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 Abstract: Cellular proteostasis requires transport of polypeptides across membranes. Although defective transport processes trigger cytosolic rescue and quality control mechanisms that clear translocases and membranes from unproductive cargo, proteins that are synthesized within mitochondria are not accessible to these mechanisms. Mitochondrial-encoded proteins are inserted cotranslationally into the inner membrane by the conserved insertase OXA1L. Here, we identify TMEM126A as a OXA1L-interacting protein. TMEM126A associates with mitochondrial ribosomes and translation products. Loss of TMEM126A leads to the destabilization of mitochondrial translation products, triggering an inner membrane quality control process, in which newly synthesized proteins are degraded by the mitochondrial iAAA protease. Our data reveal that TMEM126A cooperates with OXA1L in protein insertion into the membrane. Upon loss of TMEM126A, the cargo-blocked OXA1L insertase complexes undergo proteolytic clearance by the iAAA protease machinery together with its cargo.

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Language(s): eng - English
 Dates: 2024-01-092024-01-18
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2023.12.013
 Degree: -

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Project name : This study was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy - EXC 2067/1- 390729940 (P.R.) and CIBSS – EXC-2189 – project ID 390939984 (B.W.), SFB1190 (projects P13 [P.R.] and P23 [H.S.H.]), SFB1381 (project ID 403222702; B.W.), FOR2848 (projects P04 [P.R.] and P10 [H.S.H.], the European Research Council (ERC) Advanced Grant MiXpress (ERCAdG no. 101095062) to P.R., DFG Emmy Noether grant (RI 2715/1-1 to R.R.-D.), and the Max Planck Society (P.R.).
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Funding organization : -
Project name : MiXpress
Grant ID : 101054637
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 84 (2) Sequence Number: - Start / End Page: 345 - 358.e5 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929