Evidence map›Paper›PMID 22498477›Full record

ArticleAutophagy2012

The anti-apoptotic Bcl-B protein inhibits BECN1-dependent autophagic cell death.

Guillaume Robert, Cecile Gastaldi, Alexandre Puissant, Amine Hamouda, Arnaud Jacquel, Maeva Dufies, Nathalie Belhacene, Pascal Colosetti, John C Reed, Patrick Auberger and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Aging · 2019
    Article
  17. Article
  18. Autophagy in acute kidney injury.Kidney international · 2016
    Review
  19. Expression of Bcl-2 in canine osteosarcoma.Open veterinary journal · 2015
    Article
  20. Autophagy and apoptosis in liver injury.Cell cycle (Georgetown, Tex.) · 2015
    Review
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

11 authors at 6 institutions in 2 countries.

Guillaume RobertFaculté de Médecine, Institut Signalisation et Pathologie (IFR 50), Université de Nice Sophia-Antipolis, Nice, France.
Cecile Gastaldi
Alexandre Puissant
Amine Hamouda
Arnaud Jacquel
Maeva Dufies
Nathalie Belhacene
Pascal Colosetti
John C Reed
Patrick Auberger
Fréderic Luciano
Toxicologie, Pharmacologie et Signalisation Cellulaire · FRInserm · FRCentre Méditerranéen de Médecine Moléculaire · FRLa Ligue Contre le Cancer · FRSanford Burnham Prebys Medical Discovery Institute · USUniversité Côte d'Azur · FR

Funding

THE THERAPY OF AMLP01CA055164 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BERRY, DONALD A · 1992 to 2011
$25.3M
Mitochondria and Apoptosis (revised GM60554)R01GM060554 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI REED, JOHN C · 2000 to 2009
$3.5M
FUNCTIONAL CHARTACTERIZATION OF FINE T CELL SUBSETSR21CA081543 · NCI · STANFORD UNIVERSITY · PI HERZENBERG, LEONARD A · 1998 to 1999
–
NCI NIH HHS CA55164NCI NIH HHS CA81543NCI NIH HHS P01 CA055164NIGMS NIH HHS GM060554NIGMS NIH HHS R01 GM060554
6 · The paper itself

Abstract

Bcl-2 family members are key modulators of apoptosis that have recently been shown to also regulate autophagy. It has been previously reported that Bcl-2 and Bcl-X(L) bind and inhibit BECN1, an essential mediator of autophagy. Bcl-B is an anti-apoptotic member of the Bcl-2 family that possesses the four BH (Bcl-2 homology) domains (BH1, BH2, BH3 and BH4) and a predicted C-terminal trans-membrane domain. Although the anti-apoptotic properties of Bcl-B are well characterized, its physiological function remains to be established. In the present study, we first established that Bcl-B interacts with the BH3 domain of BECN1. We also showed that Bcl-B overexpression reduces autophagy triggered by a variety of pro-autophagic stimuli. This impairment of autophagy was closely related to the capacity of Bcl-B to bind to BECN1. Importantly, we have demonstrated that Bcl-B knockdown triggers autophagic cell death and sensitizes cells to amino acid starvation. The cell death induced by Bcl-B knockdown was partially dependent on components of the autophagy machinery (LC3; BECN1; ATG5). These findings reveal a new role of Bcl-B in the regulation of autophagy.

Indexed as

ApoptosisAutophagyAmino AcidsAmino Acid SequenceApoptosis Regulatory ProteinsBeclin-1Gene Knockdown TechniquesGene SilencingHeLa CellsHumansMembrane ProteinsMicrotubule-Associated ProteinsMolecular Sequence DataProtein BindingProtein Structure, TertiaryProto-Oncogene Proteins c-bcl-2Amino AcidsApoptosis Regulatory ProteinsBCL2-like 10 proteinBeclin-1BECN1 protein, humanMAP1LC3A protein, humanMembrane ProteinsMicrotubule-Associated ProteinsProto-Oncogene Proteins c-bcl-2

Identifiers

PMID22498477
PMCPMC3405843
OpenAlexW2067149213

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.