Evidence map›Paper›PMID 25301068›Full record

ArticleCell death and differentiation2015

Fas palmitoylation by the palmitoyl acyltransferase DHHC7 regulates Fas stability.

A Rossin, J Durivault, T Chakhtoura-Feghali, N Lounnas, L Gagnoux-Palacios, A-O Hueber

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

52 citing papers in PubMed, 79 citations in OpenAlex.

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  4. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
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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

6 authors at 1 institution in 1 country.

A RossinUniversité de Nice, Institut de Biologie Valrose, CNRS UMR 7277, INSERM UMR 1091, Nice, France.
J DurivaultUniversité de Nice, Institut de Biologie Valrose, CNRS UMR 7277, INSERM UMR 1091, Nice, France.ORCID 0000000282282915
T Chakhtoura-FeghaliUniversité de Nice, Institut de Biologie Valrose, CNRS UMR 7277, INSERM UMR 1091, Nice, France.
N LounnasUniversité de Nice, Institut de Biologie Valrose, CNRS UMR 7277, INSERM UMR 1091, Nice, France.
L Gagnoux-PalaciosUniversité de Nice, Institut de Biologie Valrose, CNRS UMR 7277, INSERM UMR 1091, Nice, France.
A-O HueberUniversité de Nice, Institut de Biologie Valrose, CNRS UMR 7277, INSERM UMR 1091, Nice, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The death receptor Fas undergoes a variety of post-translational modifications including S-palmitoylation. This protein acylation has been reported essential for an optimal cell death signaling by allowing both a proper Fas localization in cholesterol and sphingolipid-enriched membrane nanodomains, as well as Fas high-molecular weight complexes. In human, S-palmitoylation is controlled by 23 members of the DHHC family through their palmitoyl acyltransferase activity. In order to better understand the role of this post-translational modification in the regulation of the Fas-mediated apoptosis pathway, we performed a screen that allowed the identification of DHHC7 as a Fas-palmitoylating enzyme. Indeed, modifying DHHC7 expression by specific silencing or overexpression, respectively, reduces or enhances Fas palmitoylation and DHHC7 co-immunoprecipitates with Fas. At a functional level, DHHC7-mediated palmitoylation of Fas allows a proper Fas expression level by preventing its degradation through the lysosomes. Indeed, the decrease of Fas expression obtained upon loss of Fas palmitoylation can be restored by inhibiting the lysosomal degradation pathway. We describe the modification of Fas by palmitoylation as a novel mechanism for the regulation of Fas expression through its ability to circumvent its degradation by lysosomal proteolysis.

Indexed as

AcetyltransferasesAmino Acid SubstitutionApoptosisCell Line, TumorCycloheximidefas ReceptorHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsLipoylationLysosomesProtein Processing, Post-TranslationalProtein StabilityProtein Synthesis InhibitorsRNA InterferenceRNA, Small InterferingAcetyltransferasesCycloheximideFAS protein, humanfas ReceptorIntracellular Signaling Peptides and ProteinsProtein Synthesis InhibitorsRNA, Small InterferingZDHHC7 protein, human

Identifiers

PMID25301068
PMCPMC4356335
OpenAlexW2065228526

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.