Evidence map›Paper›PMID 24525733›Full record

ArticleCell death & disease2014

S-palmitoylation represents a novel mechanism regulating the mitochondrial targeting of BAX and initiation of apoptosis.

M Fröhlich, B Dejanovic, H Kashkar, G Schwarz, S Nussberger

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-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

36 citing papers in PubMed, 61 citations in OpenAlex.

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  7. Lipid metabolism in B cell biology.Molecular oncology · 2024
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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

5 authors at 2 institutions in 1 country.

M FröhlichInstitute of Biochemistry, Department of Chemistry and Center for Molecular Medicine, Cologne University, Zülpicher Strasse 47, Cologne 50674, Germany.
B DejanovicInstitute of Biochemistry, Department of Chemistry and Center for Molecular Medicine, Cologne University, Zülpicher Strasse 47, Cologne 50674, Germany.
H KashkarInstitute for Medical Microbiology, Immunology and Hygiene and Center for Molecular Medicine, Cologne University, Goldenfels Strasse 19-21, Cologne 50935, Germany.
G SchwarzInstitute of Biochemistry, Department of Chemistry and Center for Molecular Medicine, Cologne University, Zülpicher Strasse 47, Cologne 50674, Germany.
S Nussberger1] Institute of Biochemistry, Department of Chemistry and Center for Molecular Medicine, Cologne University, Zülpicher Strasse 47, Cologne 50674, Germany [2] Biophysics Department, Institute of Biology, University of Stuttgart, Pfaffenwaldring 57, Stuttgart 70550, Germany.
University of Cologne · DEUniversity of Stuttgart · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intrinsic pathway of apoptotic cell death is mainly mediated by the BCL-2-associated X (BAX) protein through permeabilization of the mitochondrial outer membrane (MOM) and the concomitant release of cytochrome c into the cytosol. In healthy, non-apoptotic cells, BAX is predominantly localized in the cytosol and exhibits a dynamic shuttle cycle between the cytosol and the mitochondria. Thus, the initial association with mitochondria represents a critical regulatory step enabling BAX to insert into MOMs, promoting the release of cytochrome c and ultimately resulting in apoptosis. However, the molecular mode of how BAX associates with MOMs and whether a cellular regulatory mechanism governs this process is poorly understood. Here we show that in both primary tissues and cultured cells, the association with MOMs and the proapoptotic action of BAX is controlled by its S-palmitoylation at Cys-126. A lack of BAX palmitoylation reduced BAX mitochondrial translocation, BAX oligomerization, caspase activity and apoptosis. Furthermore, ectopic expression of specific palmitoyl transferases in cultured healthy cells increases BAX S-palmitoylation and accelerates apoptosis, whereas malignant tumor cells show reduced BAX S-palmitoylation consistent with their reduced BAX-mediated proapoptotic activity. Our findings suggest that S-palmitoylation of BAX at Cys126 is a key regulatory process of BAX-mediated apoptosis.

Indexed as

ApoptosisProtein Processing, Post-TranslationalAcyltransferasesAnimalsbcl-2-Associated X ProteinB-LymphocytesChlorocebus aethiopsCOS CellsCysteineHEK293 CellsHodgkin DiseaseHumansLipoylationMiceMitochondriaMitochondrial MembranesAcyltransferasesBAX protein, humanBax protein, mousebcl-2-Associated X ProteinCysteineRecombinant Proteins

Identifiers

PMID24525733
PMCPMC3944235
OpenAlexW2058094774

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.