Evidence map›Paper›PMID 32870280›Full record

ArticleNucleic acids research2020

A 5' UTR GGN repeat controls localisation and translation of a potassium leak channel mRNA through G-quadruplex formation.

Connor J Maltby, James P R Schofield, Steven D Houghton, Ita O'Kelly, Mariana Vargas-Caballero, Katrin Deinhardt, Mark J Coldwell

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  7. Special Issue "Bioinformatics of Unusual DNA and RNA Structures".International journal of molecular sciences · 2024
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  10. Quantum tunneling time delay investigation ofJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
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  13. LAFITE Reveals the Complexity of Transcript Isoforms in Subcellular Fractions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
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  15. Article
  16. Article
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  18. Review
  19. G-quadruplexes in helminth parasites.Nucleic acids research · 2022
    Article
  20. 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

7 authors at 1 institution in 1 country.

Connor J MaltbySchool of Biological Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
James P R SchofieldSchool of Biological Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
Steven D HoughtonSchool of Biological Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
Ita O'KellyCentre for Human Development, Stem Cells and Regeneration, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
Mariana Vargas-CaballeroSchool of Biological Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
Katrin DeinhardtSchool of Biological Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
Mark J ColdwellSchool of Biological Sciences, University of Southampton, Southampton, Hampshire SO17 1BJ, UK.
University of Southampton · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H006834/1Biotechnology and Biological Sciences Research Council BB/L007576/1Biotechnology and Biological Sciences Research Council BB/L010097/1
6 · The paper itself

Abstract

RNA G-quadruplexes (G4s) are secondary structures proposed to function as regulators of post-transcriptional mRNA localisation and translation. G4s within some neuronal mRNAs are known to control distal localisation and local translation, contributing to distinct local proteomes that facilitate the synaptic remodelling attributed to normal cellular function. In this study, we characterise the G4 formation of a (GGN)13 repeat found within the 5' UTR of the potassium 2-pore domain leak channel Task3 mRNA. Biophysical analyses show that this (GGN)13 repeat forms a parallel G4 in vitro exhibiting the stereotypical potassium specificity of G4s, remaining thermostable under physiological ionic conditions. Through mouse brain tissue G4-RNA immunoprecipitation, we further confirm that Task3 mRNA forms a G4 structure in vivo. The G4 is inhibitory to translation of Task3 in vitro and is overcome through activity of a G4-specific helicase DHX36, increasing K+ leak currents and membrane hyperpolarisation in HEK293 cells. Further, we observe that this G4 is fundamental to ensuring delivery of Task3 mRNA to distal primary cortical neurites. It has been shown that aberrant Task3 expression correlates with neuronal dysfunction, we therefore posit that this G4 is important in regulated local expression of Task3 leak channels that maintain K+ leak within neurons.

Indexed as

G-Quadruplexes5' Untranslated RegionsAnimalsBrainCells, CulturedHEK293 CellsHumansMembrane PotentialsMiceMice, Inbred C57BLNeuronsPotassium ChannelsProtein TransportRNA, Messenger5' Untranslated RegionsPotassium ChannelsRNA, MessengerTASK3 protein, mouse

Identifiers

PMID32870280
PMCPMC7515701
OpenAlexW3082889449

What OpenQuestion holds

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LicenceCC BY
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.