Evidence map›Paper›PMID 24942160›Full record

ArticleThe EMBO journal2014

The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase.

Oleksandr Lytovchenko, Nataliia Naumenko, Silke Oeljeklaus, Bernhard Schmidt, Karina von der Malsburg, Markus Deckers, Bettina Warscheid, Martin van der Laan, Peter Rehling

Abstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Article
  11. Assembly of the membrane domain of ATP synthase in human mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Assembling the mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018
    Review
  14. INA complex liaises the FNature communications · 2017
    Article
  15. Regulation of the HCellular and molecular life sciences : CMLS · 2017
    Review
  16. Article
  17. Outer membrane protein functions as integrator of protein import and DNA inheritance in mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Article
  20. Power(2): the power of yeast genetics applied to the powerhouse of the cell.Trends in endocrinology and metabolism: TEM · 2015
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Oleksandr LytovchenkoDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Nataliia NaumenkoDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Silke OeljeklausDepartment of Biochemistry and Functional Proteomics, Faculty for Biology, University of Freiburg, Freiburg, Germany BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
Bernhard SchmidtDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Karina von der MalsburgInstitute for Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany.
Markus DeckersDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Bettina WarscheidDepartment of Biochemistry and Functional Proteomics, Faculty for Biology, University of Freiburg, Freiburg, Germany BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany.
Martin van der LaanBIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany Institute for Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany martin.van.der.laan@biochemie.uni-freiburg.de Peter.Rehling@medizin.uni-goettingen.de.
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany Max Planck Institute for Biophysical Chemistry, Göttingen, Germany martin.van.der.laan@biochemie.uni-freiburg.de Peter.Rehling@medizin.uni-goettingen.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial F1Fo-ATP synthase generates the bulk of cellular ATP. This molecular machine assembles from nuclear- and mitochondria-encoded subunits. Whereas chaperones for formation of the matrix-exposed hexameric F1-ATPase core domain have been identified, insight into how the nuclear-encoded F1-domain assembles with the membrane-embedded Fo-region is lacking. Here we identified the INA complex (INAC) in the inner membrane of mitochondria as an assembly factor involved in this process. Ina22 and Ina17 are INAC constituents that physically associate with the F1-module and peripheral stalk, but not with the assembled F1Fo-ATP synthase. Our analyses show that loss of Ina22 and Ina17 specifically impairs formation of the peripheral stalk that connects the catalytic F1-module to the membrane embedded Fo-domain. We conclude that INAC represents a matrix-exposed inner membrane protein complex that facilitates peripheral stalk assembly and thus promotes a key step in the biogenesis of mitochondrial F1Fo-ATP synthase.

Indexed as

Mitochondrial MembranesMitochondrial Proton-Translocating ATPasesMultiprotein ComplexesMutationProtein Structure, TertiaryProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsINA17 protein, S cerevisiaeINA22 protein, S cerevisiaeMitochondrial Proton-Translocating ATPasesMultiprotein ComplexesProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsassemblyF1Fo‐ATP synthasemitochondriaperipheral stalk

Identifiers

PMID24942160
PMCPMC4194097

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.