Evidence map›Paper›PMID 29233828›Full record

ArticleEMBO reports2018

E2F1 interacts with BCL-xL and regulates its subcellular localization dynamics to trigger cell death.

Céline Vuillier, Steven Lohard, Aurélie Fétiveau, Jennifer Allègre, Cémile Kayaci, Louise E King, Frédérique Braun, Sophie Barillé-Nion, Fabien Gautier, Laurence Dubrez and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. In Silico Isomerization Produces Apt Negative Data for VHTS Validation.Journal of chemical information and modeling · 2026
    Article
  2. BCL-2 and BCL-xL in Cancer: Regulation, Function, and Therapeutic Targeting.International journal of molecular sciences · 2026
    Review
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  5. Review
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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

13 authors at 2 institutions in 2 countries.

Céline VuillierCRCINA, INSERM, U1232, Université de Nantes, Nantes, France.
Steven LohardCRCINA, INSERM, U1232, Université de Nantes, Nantes, France.
Aurélie FétiveauCRCINA, INSERM, U1232, Université de Nantes, Nantes, France.
Jennifer AllègreLNC, INSERM, UMR866, Université de Bourgogne Franche-Comté, Dijon, France.
Cémile KayaciLNC, INSERM, UMR866, Université de Bourgogne Franche-Comté, Dijon, France.
Louise E KingWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, Manchester Academic Health Sciences Centre, University of Manchester, Manchester, UK.ORCID 0000-0003-2453-8887
Frédérique BraunCRCINA, INSERM, U1232, Université de Nantes, Nantes, France.
Sophie Barillé-NionCRCINA, INSERM, U1232, Université de Nantes, Nantes, France.
Fabien GautierCRCINA, INSERM, U1232, Université de Nantes, Nantes, France.
Laurence DubrezLNC, INSERM, UMR866, Université de Bourgogne Franche-Comté, Dijon, France.ORCID 0000-0002-7030-2181
Andrew P GilmoreWellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, Manchester Academic Health Sciences Centre, University of Manchester, Manchester, UK.ORCID 0000-0002-9988-0436
Philippe P JuinCRCINA, INSERM, U1232, Université de Nantes, Nantes, France philippe.juin@univ-nantes.fr laurent.maillet@univ-nantes.fr.ORCID 0000-0002-4997-3888
Laurent MailletCRCINA, INSERM, U1232, Université de Nantes, Nantes, France philippe.juin@univ-nantes.fr laurent.maillet@univ-nantes.fr.ORCID 0000-0002-8169-060X
Inserm · FRWellcome Centre for Cell-Matrix Research · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

E2F1 is the main pro-apoptotic effector of the pRB-regulated tumor suppressor pathway by promoting the transcription of various pro-apoptotic proteins. We report here that E2F1 partly localizes to mitochondria, where it favors mitochondrial outer membrane permeabilization. E2F1 interacts with BCL-xL independently from its BH3 binding interface and induces a stabilization of BCL-xL at mitochondrial membranes. This prevents efficient control of BCL-xL over its binding partners, in particular over BAK resulting in the induction of cell death. We thus identify a new, non-BH3-binding regulator of BCL-xL localization dynamics that influences its anti-apoptotic activity.

Indexed as

Cell DeathApoptosisbcl-2 Homologous Antagonist-Killer Proteinbcl-X ProteinCell Line, TumorE2F1 Transcription FactorExtracellular SpaceGene Expression RegulationHumansMitochondriaProtein BindingProtein TransportProto-Oncogene Proteins c-bcl-2Transcription, GeneticBAK1 protein, humanbcl-2 Homologous Antagonist-Killer ProteinBCL2L1 protein, humanbcl-X ProteinE2F1 protein, humanE2F1 Transcription FactorProto-Oncogene Proteins c-bcl-2apoptosisBCL‐2 familyBCL‐xL mobilityE2F1

Identifiers

PMID29233828
PMCPMC5797968
OpenAlexW2773012738

What OpenQuestion holds

Textmetadata
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.