Evidence map›Paper›PMID 35023587›Full record

ArticleThe EMBO journal2022

DRP1 interacts directly with BAX to induce its activation and apoptosis.

Andreas Jenner, Aida Peña-Blanco, Raquel Salvador-Gallego, Begoña Ugarte-Uribe, Cristiana Zollo, Tariq Ganief, Jan Bierlmeier, Markus Mund, Jason E Lee, Jonas Ries and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed, 1 pooled it
11.9field-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

89 citing papers in PubMed, 1 synthesis or guideline pooled it, 139 citations in OpenAlex.

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  10. MTCH2 promotes BAX and BAK self-assembly and apoptotic pore growth.Nature structural & molecular biology · 2026
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29 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

13 authors at 4 institutions in 2 countries.

Andreas JennerInstitute for Genetics, CECAD, University of Cologne, Cologne, Germany.ORCID 0000-0002-6388-3053
Aida Peña-Blanco *Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Raquel Salvador-Gallego *Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-1447-2303
Begoña Ugarte-Uribe *Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Cristiana Zollo *Institute for Genetics, CECAD, University of Cologne, Cologne, Germany.ORCID 0000-0002-8747-1344
Tariq GaniefInterfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Jan BierlmeierInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-7261-4744
Markus MundCell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0001-6449-743X
Jason E LeeUniversity of Colorado, Boulder, CO, USA.ORCID 0000-0001-5757-5954
Jonas RiesCell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0002-6640-9250
Dirk SchwarzerInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-7477-3319
Boris MacekInterfaculty Institute of Cell Biology, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-1206-2458
Ana J Garcia-SaezInstitute for Genetics, CECAD, University of Cologne, Cologne, Germany.ORCID 0000-0002-3894-5945
University of Tübingen · DEUniversity of Cologne · DEEuropean Molecular Biology Laboratory · DEUniversity of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The apoptotic executioner protein BAX and the dynamin-like protein DRP1 co-localize at mitochondria during apoptosis to mediate mitochondrial permeabilization and fragmentation. However, the molecular basis and functional consequences of this interplay remain unknown. Here, we show that BAX and DRP1 physically interact, and that this interaction is enhanced during apoptosis. Complex formation between BAX and DRP1 occurs exclusively in the membrane environment and requires the BAX N-terminal region, but also involves several other BAX surfaces. Furthermore, the association between BAX and DRP1 enhances the membrane activity of both proteins. Forced dimerization of BAX and DRP1 triggers their activation and translocation to mitochondria, where they induce mitochondrial remodeling and permeabilization to cause apoptosis even in the absence of apoptotic triggers. Based on this, we propose that DRP1 can promote apoptosis by acting as noncanonical direct activator of BAX through physical contacts with its N-terminal region.

Indexed as

ApoptosisDynaminsbcl-2-Associated X ProteinMitochondriabcl-2-Associated X ProteinDynaminsBCL-2 proteinsfluorescence correlation spectroscopymembrane protein complexmitochondrial divisionsuper-resolution microscopy

Identifiers

PMID35023587
PMCPMC9016351
OpenAlexW4205280413

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.