Evidence map›Paper›PMID 29593233›Full record

ArticleScientific reports2018

Mechanism of translation control of the alternative Drosophila melanogaster Voltage Dependent Anion-selective Channel 1 mRNAs.

L Leggio, F Guarino, A Magrì, R Accardi-Gheit, S Reina, V Specchia, F Damiano, M F Tomasello, M Tommasino, A Messina

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Developing a Novel and Optimized Yeast Model for Human VDAC Research.International journal of molecular sciences · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. High-Resolution Respirometry Reveals MPPInternational journal of molecular sciences · 2020
    Article
  10. Review
  11. Article
  12. Frontiers in plant science · 2020
    Article
  13. 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

10 authors at 4 institutions in 2 countries.

L LeggioDepartment of Biological, University of Catania, Geological and Environmental Sciences, Catania, 95125, Italy.
F GuarinoDepartment of Biomedical and Biotechnological Sciences, University of Catania, Catania, 95123, Italy.
A MagrìDepartment of Biological, University of Catania, Geological and Environmental Sciences, Catania, 95125, Italy.
R Accardi-GheitInternational Agency for Research on Cancer (IARC), World Health Organization, Lyon, 69372, France.
S ReinaDepartment of Biological, University of Catania, Geological and Environmental Sciences, Catania, 95125, Italy.
V SpecchiaDepartment of Biological and Environmental Sciences and Technologies (DiSTeBA), University of Salento, Lecce, Italy.
F DamianoDepartment of Biological and Environmental Sciences and Technologies (DiSTeBA), University of Salento, Lecce, Italy.ORCID 0000-0001-7828-9519
M F TomaselloIBB-CNR, Institute of Biostructure and Bioimaging, Section of Catania, Via Paolo Gaifami, 18-95126, Catania, Italy.
M TommasinoInternational Agency for Research on Cancer (IARC), World Health Organization, Lyon, 69372, France.
A MessinaDepartment of Biological, University of Catania, Geological and Environmental Sciences, Catania, 95125, Italy. mess@unict.it.
University of Catania · ITCentre international de recherche sur le cancer · FRUniversity of Salento · ITInstitute of Biostructure and Bioimaging · IT

Funding

Wellcome TrustWorld Health Organization 001
6 · The paper itself

Abstract

The eukaryotic porin, also called the Voltage Dependent Anion-selective Channel (VDAC), is the main pore-forming protein of the outer mitochondrial membrane. In Drosophila melanogaster, a cluster of genes evolutionarily linked to VDAC is present on chromosome 2L. The main VDAC isoform, called VDAC1 (Porin1), is expressed from the first gene of the cluster. The porin1 gene produces two splice variants, 1A-VDAC and 1B-VDAC, with the same coding sequence but different 5' untranslated regions (UTRs). Here, we studied the influence of the two 5' UTRs, 1A-5' UTR and 1B-5' UTR, on transcription and translation of VDAC1 mRNAs. In porin-less yeast cells, transformation with a construct carrying 1A-VDAC results in the expression of the corresponding protein and in complementation of a defective cell phenotype, whereas the 1B-VDAC sequence actively represses VDAC expression. Identical results were obtained using constructs containing the two 5' UTRs upstream of the GFP reporter. A short region of 15 nucleotides in the 1B-5' UTR should be able to pair with an exposed helix of 18S ribosomal RNA (rRNA), and this interaction could be involved in the translational repression. Our data suggest that contacts between the 5' UTR and 18S rRNA sequences could modulate the translation of Drosophila 1B-VDAC mRNA. The evolutionary significance of this finding is discussed.

Indexed as

Gene Expression RegulationProtein Biosynthesis5' Untranslated RegionsAnimalsDrosophila melanogasterGenes, ReporterNucleic Acid ConformationNucleotide MotifsOpen Reading FramesProtein ConformationRNA, MessengerRNA, Ribosomal, 18SVoltage-Dependent Anion Channel 1Yeasts5' Untranslated RegionsRNA, MessengerRNA, Ribosomal, 18SVoltage-Dependent Anion Channel 1

Identifiers

PMID29593233
PMCPMC5871876
OpenAlexW2806291212

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.