Evidence map›Paper›PMID 22513091›Full record

ArticleMolecular biology of the cell2012

The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates.

Stefan Stoldt, Dirk Wenzel, Markus Hildenbeutel, Christian A Wurm, Johannes M Herrmann, Stefan Jakobs

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
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

12 citing papers in PubMed, 36 citations in OpenAlex.

  1. PKAN pathogenesis and treatment.Molecular genetics and metabolism · 2022
    Review
  2. Review
  3. Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021
    Review
  4. Review
  5. Light Microscopy of Mitochondria at the Nanoscale.Annual review of biophysics · 2020
    Review
  6. Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    Review
  10. Superresolution microscopy reveals spatial separation of UCP4 and F0F1-ATP synthase in neuronal mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Article
  12. STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Stefan StoldtDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. sjakobs@gwdg.de
Dirk Wenzel
Markus Hildenbeutel
Christian A Wurm
Johannes M Herrmann
Stefan Jakobs
Max Planck Institute for Biophysical Chemistry · DEUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Oxa1 protein is a well-conserved integral protein of the inner membrane of mitochondria. It mediates the insertion of both mitochondrial- and nuclear-encoded proteins from the matrix into the inner membrane. We investigated the distribution of budding yeast Oxa1 between the two subdomains of the contiguous inner membrane--the cristae membrane (CM) and the inner boundary membrane (IBM)--under different physiological conditions. We found that under fermentable growth conditions, Oxa1 is enriched in the IBM, whereas under nonfermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; similarly, deletion of the ribosome-binding domain of Oxa1 prevents an enrichment of Oxa1 in the CM. The predominant localization in the IBM under fermentable growth conditions is prevented by inhibiting mitochondrial protein import. Furthermore, overexpression of the nuclear-encoded Oxa1 substrate Mdl1 shifts the distribution of Oxa1 toward the IBM. Apparently, the availability of nuclear- and mitochondrial-encoded substrates influences the inner-membrane distribution of Oxa1. Our findings show that the distribution of Oxa1 within the inner membrane is dynamic and adapts to different physiological needs.

Indexed as

ATP-Binding Cassette TransportersCarbonCell NucleusElectron Transport Complex IVGreen Fluorescent ProteinsImmunoblottingLuminescent ProteinsMembrane ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceMicroscopy, ImmunoelectronMitochondriaMitochondrial MembranesMitochondrial ProteinsMutationNuclear ProteinsATP-Binding Cassette TransportersCarbonElectron Transport Complex IVGreen Fluorescent ProteinsLuminescent ProteinsMDL1 protein, S cerevisiaeMDM10 protein, S cerevisiaeMembrane ProteinsMitochondrial ProteinsNuclear ProteinsOXA1 proteinRed Fluorescent ProteinSaccharomyces cerevisiae Proteins

Identifiers

PMID22513091
PMCPMC3374748
OpenAlexW2165380067

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.