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Research Article
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MIC26 and MIC27 cooperate to regulate cardiolipin levels and the landscape of OXPHOS complexes

View ORCID ProfileRuchika Anand  Correspondence email, View ORCID ProfileArun Kumar Kondadi, Jana Meisterknecht, View ORCID ProfileMathias Golombek, Oliver Nortmann, Julia Riedel, Leon Peifer-Weiß, Nahal Brocke-Ahmadinejad, David Schlütermann, Björn Stork, Thomas O Eichmann, Ilka Wittig, View ORCID ProfileAndreas S Reichert  Correspondence email
Ruchika Anand
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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  • ORCID record for Ruchika Anand
  • For correspondence: anand@hhu.de
Arun Kumar Kondadi
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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  • ORCID record for Arun Kumar Kondadi
Jana Meisterknecht
2Functional Proteomics, Sonderforschungsbereich (SFB) 815 Core Unit, Faculty of Medicine, Goethe-University, Frankfurt am Main, Germany
3Cluster of Excellence “Macromolecular Complexes”, Goethe University, Frankfurt am Main, Germany
4German Center of Cardiovascular Research (DZHK), Partner Site RheinMain, Frankfurt, Germany
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Mathias Golombek
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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  • ORCID record for Mathias Golombek
Oliver Nortmann
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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Julia Riedel
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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Leon Peifer-Weiß
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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Nahal Brocke-Ahmadinejad
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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David Schlütermann
5Institute of Molecular Medicine I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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Björn Stork
5Institute of Molecular Medicine I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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Thomas O Eichmann
6Center for Explorative Lipidomics, BioTechMed-Graz, Graz, Austria
7Institute of Molecular Biosciences, University of Graz, Graz, Austria
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Ilka Wittig
2Functional Proteomics, Sonderforschungsbereich (SFB) 815 Core Unit, Faculty of Medicine, Goethe-University, Frankfurt am Main, Germany
3Cluster of Excellence “Macromolecular Complexes”, Goethe University, Frankfurt am Main, Germany
4German Center of Cardiovascular Research (DZHK), Partner Site RheinMain, Frankfurt, Germany
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Andreas S Reichert
1Institute of Biochemistry and Molecular Biology I, Heinrich Heine University Düsseldorf, Medical Faculty, Düsseldorf, Germany
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  • ORCID record for Andreas S Reichert
  • For correspondence: reichert@hhu.de
Published 11 August 2020. DOI: 10.26508/lsa.202000711
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Abstract

Homologous apolipoproteins of MICOS complex, MIC26 and MIC27, show an antagonistic regulation of their protein levels, making it difficult to deduce their individual functions using a single gene deletion. We obtained single and double knockout (DKO) human cells of MIC26 and MIC27 and found that DKO show more concentric onion-like cristae with loss of CJs than any single deletion indicating overlapping roles in formation of CJs. Using a combination of complexome profiling, STED nanoscopy, and blue-native gel electrophoresis, we found that MIC26 and MIC27 are dispensable for the stability and integration of the remaining MICOS subunits into the complex suggesting that they assemble late into the MICOS complex. MIC26 and MIC27 are cooperatively required for the integrity of respiratory chain (super) complexes (RCs/SC) and the F1Fo–ATP synthase complex and integration of F1 subunits into the monomeric F1Fo–ATP synthase. While cardiolipin was reduced in DKO cells, overexpression of cardiolipin synthase in DKO restores the stability of RCs/SC. Overall, we propose that MIC26 and MIC27 are cooperatively required for global integrity and stability of multimeric OXPHOS complexes by modulating cardiolipin levels.

  • Received March 20, 2020.
  • Revision received July 20, 2020.
  • Accepted July 21, 2020.
  • © 2020 Anand et al.
Creative Commons logoCreative Commons logohttps://creativecommons.org/licenses/by/4.0/

This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

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MIC26 and MIC27 regulate OXPHOS complexes
Ruchika Anand, Arun Kumar Kondadi, Jana Meisterknecht, Mathias Golombek, Oliver Nortmann, Julia Riedel, Leon Peifer-Weiß, Nahal Brocke-Ahmadinejad, David Schlütermann, Björn Stork, Thomas O Eichmann, Ilka Wittig, Andreas S Reichert
Life Science Alliance Aug 2020, 3 (10) e202000711; DOI: 10.26508/lsa.202000711

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MIC26 and MIC27 regulate OXPHOS complexes
Ruchika Anand, Arun Kumar Kondadi, Jana Meisterknecht, Mathias Golombek, Oliver Nortmann, Julia Riedel, Leon Peifer-Weiß, Nahal Brocke-Ahmadinejad, David Schlütermann, Björn Stork, Thomas O Eichmann, Ilka Wittig, Andreas S Reichert
Life Science Alliance Aug 2020, 3 (10) e202000711; DOI: 10.26508/lsa.202000711
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Volume 3, No. 10
October 2020
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