Evidence map›Paper›PMID 30714902›Full record

ArticleeLife2019

Molecular and topological reorganizations in mitochondrial architecture interplay during Bax-mediated steps of apoptosis.

Nicholas R Ader, Patrick C Hoffmann, Iva Ganeva, Alicia C Borgeaud, Chunxin Wang, Richard J Youle, Wanda Kukulski

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 105 citations in OpenAlex.

  1. A planar dimer of bovine ATP synthase.Cell death and differentiation · 2026
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  8. In situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

7 authors at 2 institutions in 2 countries.

Nicholas R AderCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0001-7744-4484
Patrick C HoffmannCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0003-3421-6363
Iva GanevaCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0003-3221-2502
Alicia C BorgeaudCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0002-7231-7424
Chunxin WangBiochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.ORCID 0000-0001-6015-6806
Richard J YouleBiochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.ORCID 0000-0001-9117-5241
Wanda KukulskiCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0002-2778-3936
MRC Laboratory of Molecular Biology · GBNational Institutes of Health · US

Funding

Targeting Protein Aggregates for Autophagosomal DegradationZIANS002859 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI YOULE, RICHARD JAMES · 2009 to 2025
$16.1M
Medical Research Council MC_UP_1201/8NIH HHS Oxford-Cambridge Scholars ProgramNINDS NIH HHS Intramural Research Progam
6 · The paper itself

Abstract

During apoptosis, Bcl-2 proteins such as Bax and Bak mediate the release of pro-apoptotic proteins from the mitochondria by clustering on the outer mitochondrial membrane and thereby permeabilizing it. However, it remains unclear how outer membrane openings form. Here, we combined different correlative microscopy and electron cryo-tomography approaches to visualize the effects of Bax activity on mitochondria in human cells. Our data show that Bax clusters localize near outer membrane ruptures of highly variable size. Bax clusters contain structural elements suggesting a higher order organization of their components. Furthermore, unfolding of inner membrane cristae is coupled to changes in the supramolecular assembly of ATP synthases, particularly pronounced at membrane segments exposed to the cytosol by ruptures. Based on our results, we propose a comprehensive model in which molecular reorganizations of the inner membrane and sequestration of outer membrane components into Bax clusters interplay in the formation of outer membrane ruptures. Editorial note: This article has been through an editorial process in which the authors decide how to respond to the issues raised during peer review. The Reviewing Editor's assessment is that all the issues have been addressed (see decision letter).

Indexed as

Apoptosisbcl-2-Associated X ProteinCryoelectron MicroscopyCytosolHeLa CellsHumansMitochondriaMitochondrial MembranesMitochondrial Proton-Translocating ATPasesProtein MultimerizationProtein TransportProto-Oncogene Proteins c-bcl-2BAX protein, humanbcl-2-Associated X ProteinMitochondrial Proton-Translocating ATPasesProto-Oncogene Proteins c-bcl-2apoptosisBaxcell biologyCLEMcryo focused ion beamelectron cryo-tomographyhumanmitochondriamolecular biophysicsstructural biology

Identifiers

PMID30714902
PMCPMC6361589
OpenAlexW2952024915

What OpenQuestion holds

Textmetadata
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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.