Evidence map›Paper›PMID 35585181›Full record

ArticleCell death and differentiation2022

Apoptotic priming is defined by the dynamic exchange of Bcl-2 proteins between mitochondria and cytosol.

Louise E King, Ricardo Rodriguez-Enriquez, Robert Pedley, Charlotte E L Mellor, Pengbo Wang, Egor Zindy, Michael R H White, Keith Brennan, Andrew P Gilmore

Open access · hybridAbstract read
In one paragraph

Article in Cell death and differentiation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. BCL-2 and BCL-xL in Cancer: Regulation, Function, and Therapeutic Targeting.International journal of molecular sciences · 2026
    Review
  3. Mitochondrial regulation of cellular senescence heterogeneity.Frontiers in cell and developmental biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Mechanisms of BCL-2 family proteins in mitochondrial apoptosis.Nature reviews. Molecular cell biology · 2023
    Review
  12. Review
  13. 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

9 authors at 6 institutions in 4 countries.

Louise E King *Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Ricardo Rodriguez-Enriquez *Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Robert PedleyWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.ORCID 0000-0002-0801-7240
Charlotte E L MellorWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Pengbo WangWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Egor ZindyWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Michael R H WhiteDivision of Molecular and Cellular Function, Faculty of Biology, Medicine and Health, Manchester Academic Health Sciences Centre, University of Manchester, Manchester, UK.
Keith BrennanDivision of Cancer Sciences, University of Manchester, Manchester, UK.ORCID 0000-0002-9384-125X
Andrew P GilmoreWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK. agilmore@manchester.ac.uk.ORCID 0000-0002-9988-0436
Wellcome Centre for Cell-Matrix Research · GBManchester Academic Health Science Centre · GBSt. Jude Children's Research Hospital · USUniversité Libre de Bruxelles · BEUniversity of Cologne · DEUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UKMedical Research Council MR/L011840/1Wellcome TrustWellcome Trust (Wellcome) 088785/Z/09/ZWellcome Trust (Wellcome) 204796/Z/16/Z
6 · The paper itself

Abstract

Apoptosis is regulated by interactions between the BH3-only and multi-domain Bcl-2 family proteins. These interactions are integrated on the outer mitochondrial membrane (OMM) where they set the threshold for apoptosis, known as mitochondrial priming. However, how mitochondrial priming is controlled at the level of single cells remains unclear. Retrotranslocation of Bcl-XL has been proposed as one mechanism, removing pro-apoptotic Bcl-2 proteins from the OMM, thus reducing priming. Contrary to this view, we now show that Bcl-XL retrotranslocation is inhibited by binding to its BH3-only partners, resulting in accumulation of these protein complexes on mitochondria. We find that Bcl-XL retrotranslocation dynamics are tightly coupled to mitochondrial priming. Quantifying these dynamics indicates the heterogeneity in priming between cells within a population and predicts how they subsequently respond to a pro-apoptotic signal.

Indexed as

MitochondriaProto-Oncogene Proteins c-bcl-2ApoptosisApoptosis Regulatory Proteinsbcl-2-Associated X Proteinbcl-X ProteinCytosolMitochondrial MembranesApoptosis Regulatory Proteinsbcl-2-Associated X Proteinbcl-X ProteinProto-Oncogene Proteins c-bcl-2

Identifiers

PMID35585181
PMCPMC9613888
OpenAlexW4280608246

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.