Evidence map›Paper›PMID 26271728›Full record

ArticleNature communications2015

Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species.

Yamunadevi Subburaj, Katia Cosentino, Markus Axmann, Esteban Pedrueza-Villalmanzo, Eduard Hermann, Stephanie Bleicken, Joachim Spatz, Ana J García-Sáez

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

100 citing papers in PubMed, 181 citations in OpenAlex.

  1. AFM to Study Pore-Forming Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
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  5. Frontiers in microbiology · 2026
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  16. Mitochondria and cell death.Nature cell biology · 2024
    Review
  17. Review
  18. Article
  19. Article
  20. Review

40 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Yamunadevi SubburajMembrane Biophysics, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany.
Katia Cosentino1] Membrane Biophysics, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany [2] Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Strasse 4, 72076 Tuebingen, Germany.
Markus AxmannNew Materials and Biosystems, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany.
Esteban Pedrueza-Villalmanzo1] Membrane Biophysics, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany [2] Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Strasse 4, 72076 Tuebingen, Germany.
Eduard Hermann1] Membrane Biophysics, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany [2] Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Strasse 4, 72076 Tuebingen, Germany.
Stephanie Bleicken1] Membrane Biophysics, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany [2] Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Strasse 4, 72076 Tuebingen, Germany.
Joachim SpatzNew Materials and Biosystems, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany.
Ana J García-Sáez1] Membrane Biophysics, Max Planck Institute for Intelligent Systems, Heisenbergstrasse 3, 70569 Stuttgart, Germany [2] Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Strasse 4, 72076 Tuebingen, Germany.
Max Planck Institute for Intelligent Systems · DEUniversity of Tübingen · DE

Funding

Austrian Science Fund FWF J 3086European Research Council 309966
6 · The paper itself

Abstract

Bax is a key regulator of apoptosis that mediates the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation. However, the molecular mechanism of Bax assembly and regulation by other Bcl-2 members remains obscure. Here, by analysing the stoichiometry of Bax oligomers at the single-molecule level, we find that Bax binds to the membrane in a monomeric state and then self-assembles in <1 min. Strikingly, active Bax does not exist in a unique oligomeric state, but as several different species based on dimer units. Moreover, we show that cBid activates Bax without affecting its assembly, while Bcl-xL induces the dissociation of Bax oligomers. On the basis of our experimental data and theoretical modelling, we propose a new mechanism for the molecular pathway of Bax assembly to form the apoptotic pore.

Indexed as

bcl-2-Associated X ProteinLipid BilayersMicroscopyProtein BindingSpectrometry, Fluorescencebcl-2-Associated X ProteinLipid Bilayers

Identifiers

PMID26271728
PMCPMC4557355
OpenAlexW1915252789

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.