Evidence map›Paper›PMID 19074440›Full record

ArticleThe Journal of biological chemistry2009

Endophilin B1/Bif-1 stimulates BAX activation independently from its capacity to produce large scale membrane morphological rearrangements.

Aitor Etxebarria, Oihana Terrones, Hirohito Yamaguchi, Ane Landajuela, Olatz Landeta, Bruno Antonsson, Hong-Gang Wang, Gorka Basañez

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
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  7. The engagement of autophagy in maniac disease.CNS neuroscience & therapeutics · 2023
    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

8 authors at 4 institutions in 3 countries.

Aitor EtxebarriaUnidad de Biofísica, Centro Mixto Consejo Superior de Investigaciones Cientificas, Universidad del Pais Vasco/Euskal Herriko Unibertsitatea, 48080 Bilbao, Spain.
Oihana Terrones
Hirohito Yamaguchi
Ane Landajuela
Olatz Landeta
Bruno Antonsson
Hong-Gang Wang
Gorka Basañez
University of the Basque Country · ESMerck (Germany) · DEPennsylvania State University · USThe University of Texas MD Anderson Cancer Center · US

Funding

POSTTRANSLATIONAL MODIFICATIONS OF BADR01CA082197 · NCI · UNIVERSITY OF SOUTH FLORIDA · PI WANG, HONG-GANG · 1999 to 2015
$3.3M
NCI NIH HHS R01 CA082197
6 · The paper itself

Abstract

Endophilin B1/BAX-interacting factor 1 (Bif-1) is a protein that cooperates with dynamin-like protein 1 (DLP1/Drp1) to maintain normal mitochondrial outer membrane (MOM) dynamics in healthy cells and also contributes to BAX-driven MOM permeabilization (MOMP), the irreversible commitment point to cell death for the majority of apoptotic stimuli. However, despite its importance, exactly how Bif-1 fulfils its proapoptotic role is unknown. Here, we demonstrate that the stimulatory effect of Bif-1 on BAX-driven MOMP and on BAX conformational activation observed in intact cells during apoptosis can be recapitulated in a simplified system consisting of purified proteins and MOM-like liposomes. In this reconstituted model system the N-BAR domain of Bif-1 reproduced the stimulatory effect of Bif-1 on functional BAX activation. This process was dependent on physical interaction between Bif-1 N-BAR and BAX as well as on the presence of the mitochondrion-specific lipid cardiolipin. Despite that Bif-1 N-BAR produced large scale morphological rearrangements in MOM-like liposomes, this phenomenon could be separated from functional BAX activation. Furthermore, DLP1 also caused global morphological changes in MOM-like liposomes, but DLP1 did not stimulate BAX-permeabilizing function in the absence or presence of Bif-1. Taken together, our findings not only provide direct evidence for a functional interplay between Bif-1, BAX, and cardiolipin during MOMP but also add significantly to the growing body of evidence indicating that components of the mitochondrial morphogenesis machinery possess proapoptotic functions that are independent from their recognized roles in normal mitochondrial dynamics.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsApoptosisbcl-2-Associated X ProteinCardiolipinsDynaminsGTP PhosphohydrolasesHumansLiposomesMaleMicrotubule-Associated ProteinsMitochondria, LiverMitochondrial MembranesMitochondrial ProteinsModels, BiologicalProtein Structure, TertiaryAdaptor Proteins, Signal TransducingBAX protein, humanBax protein, ratbcl-2-Associated X ProteinCardiolipinsDNM1L protein, humanDnm1l protein, ratDynaminsGTP PhosphohydrolasesLiposomesMicrotubule-Associated ProteinsMitochondrial ProteinsSH3GLB1 protein, human

Identifiers

PMID19074440
PMCPMC3837389
OpenAlexW2041101236

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.