Evidence map›Paper›PMID 40545711›Full record

ArticleProtein science : a publication of the Protein Society2025

The dual-coding gene SLC35A4 protects against oxidative stress.

Ikram Ajala, Imadeddine Tiaiba, Benoît Grondin, Damien Lipuma, Souleimen Jmii, Hiba Benlyamani, Laurent Cappadocia, Benoît Vanderperre

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. The dual-coding gene SLC35A4 protects against oxidative stress.Protein science : a publication of the Protein Society · 2025
    Article
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.

Ikram AjalaDépartement des Sciences Biologiques, Université du Québec à Montréal, Montréal, Quebec, Canada.ORCID 0000-0001-5821-3859
Imadeddine TiaibaDépartement des Sciences Biologiques, Université du Québec à Montréal, Montréal, Quebec, Canada.
Benoît GrondinDépartement des Sciences Biologiques, Université du Québec à Montréal, Montréal, Quebec, Canada.
Damien LipumaDépartement des Sciences Biologiques, Université du Québec à Montréal, Montréal, Quebec, Canada.
Souleimen JmiiNetwork for Research on Protein Function, Engineering and Applications (PROTEO), Montréal, Quebec, Canada.
Hiba BenlyamaniDépartement des Sciences Biologiques, Université du Québec à Montréal, Montréal, Quebec, Canada.
Laurent CappadociaCentre d'Excellence de Recherche sur les Maladies Orphelines - Fondation Courtois (CERMO-FC), Montréal, Quebec, Canada.ORCID 0000-0001-7348-1982
Benoît VanderperreDépartement des Sciences Biologiques, Université du Québec à Montréal, Montréal, Quebec, Canada.ORCID 0000-0002-2111-1071

Funding

Centre d'Excellence en Recherche sur les Maladies Orphelines - Fondation CourtoisNatural Sciences and Engineering Research Council of Canada RGPIN-2021-03723Regroupement Québécois de Recherche sur la Fonction, l'Ingénierie et les Applications des Protéines (PROTEO) - Fonds de recherche du Québec 341121
6 · The paper itself

Abstract

Alternative proteins (AltProts) represent a newly recognized class of biologically active proteins encoded from alternative open reading frames (AltORFs) within already annotated genes. This study focuses on the SLC35A4 gene, which encodes both the reference protein SLC35A4 and the alternative protein AltSLC35A4. Using a combination of microscopy and biochemical analyses, we confirmed the presence of AltSLC35A4 in the inner mitochondrial membrane, resolving previous conflicting reports. Previous studies employing ribosome profiling have revealed that during oxidative stress induced by sodium arsenite, the reference coding sequence of SLC35A4 exhibits the largest increase in translational efficiency among all cellular mRNAs. Our results confirmed this translational upregulation, with the emergence of SLC35A4 protein isoforms during oxidative stress in an upstream ORF-dependent manner. Notably, the expression of AltSLC35A4 remained unchanged during oxidative stress. Knock out of SLC35A4 or AltSLC35A4 enhanced sensitivity to oxidative stress in a rescuable manner, indicating a direct implication for these proteins in stress resistance. In conclusion, our research provides compelling evidence for the functional significance of the dual-coding nature of SLC35A4 for resistance to oxidative stress and highlights the importance of considering AltProts in the functional study of eukaryotic genes.

Indexed as

Oxidative StressArsenitesHumansOpen Reading FramesProtein BiosynthesisArsenitesAltSLC35A4bicistronic eukaryotic geneintegrated stress responseoxidative stresstranslational regulation

Identifiers

PMID40545711
PMCPMC12183330

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.