Evidence map›Paper›PMID 32040548›Full record

ArticleThe Journal of cell biology2020

Syncrip/hnRNP Q is required for activity-induced Msp300/Nesprin-1 expression and new synapse formation.

Joshua Titlow, Francesca Robertson, Aino Järvelin, David Ish-Horowicz, Carlas Smith, Enrico Gratton, Ilan Davis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. From development to disease: the neuronal role of hnRNPs through the lens ofFrontiers in cell and developmental biology · 2026
    Review
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  15. BiallelicGenes · 2021
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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

7 authors at 2 institutions in 2 countries.

Joshua TitlowDepartment of Biochemistry, University of Oxford, Oxford, UK.
Francesca RobertsonDepartment of Biochemistry, University of Oxford, Oxford, UK.
Aino JärvelinDepartment of Biochemistry, University of Oxford, Oxford, UK.
David Ish-HorowiczDepartment of Biochemistry, University of Oxford, Oxford, UK.
Carlas SmithCentre for Neural Circuits and Behaviour, University of Oxford, Oxford, UK.
Enrico GrattonLaboratory for Fluorescence Dynamics, University of California Irvine, Irvine, CA.
Ilan DavisDepartment of Biochemistry, University of Oxford, Oxford, UK.
University of Oxford · GBFluor (United States) · US

Funding

TRD4: Phasor analysisP41GM103540 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GRATTON, ENRICO · 2012 to 2020
$12.5M
Medical Research CouncilNIGMS NIH HHS P41 GM103540Wellcome Trust 091911Wellcome Trust 096144Wellcome Trust 107457Wellcome Trust 209412Wellcome Trust 209412/Z/17/Z
6 · The paper itself

Abstract

Memory and learning involve activity-driven expression of proteins and cytoskeletal reorganization at new synapses, requiring posttranscriptional regulation of localized mRNA a long distance from corresponding nuclei. A key factor expressed early in synapse formation is Msp300/Nesprin-1, which organizes actin filaments around the new synapse. How Msp300 expression is regulated during synaptic plasticity is poorly understood. Here, we show that activity-dependent accumulation of Msp300 in the postsynaptic compartment of the Drosophila larval neuromuscular junction is regulated by the conserved RNA binding protein Syncrip/hnRNP Q. Syncrip (Syp) binds to msp300 transcripts and is essential for plasticity. Single-molecule imaging shows that msp300 is associated with Syp in vivo and forms ribosome-rich granules that contain the translation factor eIF4E. Elevated neural activity alters the dynamics of Syp and the number of msp300:Syp:eIF4E RNP granules at the synapse, suggesting that these particles facilitate translation. These results introduce Syp as an important early acting activity-dependent regulator of a plasticity gene that is strongly associated with human ataxias.

Indexed as

Neuronal PlasticityAnimalsAnimals, Genetically ModifiedDrosophila melanogasterDrosophila ProteinsEukaryotic Initiation Factor-4EGene Expression Regulation, DevelopmentalMicrofilament ProteinsMuscle ProteinsMuscle, SkeletalNeuromuscular JunctionRNA-Binding ProteinsTime FactorsDrosophila ProteinsEukaryotic Initiation Factor-4EMicrofilament ProteinsMsp300 protein, DrosophilaMuscle ProteinsRNA-Binding ProteinsSyp protein, Drosophila

Identifiers

PMID32040548
PMCPMC7055005
OpenAlexW3005703665

What OpenQuestion holds

Textmetadata
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.