Evidence map›Paper›PMID 31197139›Full record

ArticleNature communications2019

The prion-like domain of Drosophila Imp promotes axonal transport of RNP granules in vivo.

Jeshlee Vijayakumar, Charlène Perrois, Marjorie Heim, Luc Bousset, Simon Alberti, Florence Besse

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Liquid-liquid phase separation in neural development.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Emerging Roles of RNA-Binding Proteins in Neurodevelopment.Journal of developmental biology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Review
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 3 institutions in 2 countries.

Jeshlee VijayakumarUniversity Côte d'Azur, CNRS, Inserm, iBV, Nice, 06100, France.
Charlène PerroisUniversity Côte d'Azur, CNRS, Inserm, iBV, Nice, 06100, France.
Marjorie HeimUniversity Côte d'Azur, CNRS, Inserm, iBV, Nice, 06100, France.ORCID http://orcid.org/0000-0002-7858-4822
Luc BoussetParis-Saclay Institute of Neuroscience, Orsay, 91505, France.
Simon AlbertiMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, 01307, Germany.ORCID http://orcid.org/0000-0003-4017-6505
Florence BesseUniversity Côte d'Azur, CNRS, Inserm, iBV, Nice, 06100, France. besse@unice.fr.ORCID http://orcid.org/0000-0003-4672-1068
Centre National de la Recherche Scientifique · FRCenter for Systems Biology Dresden · DEInstitut des Neurosciences Paris-Saclay · FR

Funding

Agence Nationale de la Recherche (French National Research Agency) RNAGRIMPFondation ARC pour la Recherche sur le Cancer (ARC Foundation for Cancer Research) PJA 20141201623
6 · The paper itself

Abstract

Prion-like domains (PLDs), defined by their low sequence complexity and intrinsic disorder, are present in hundreds of human proteins. Although gain-of-function mutations in the PLDs of neuronal RNA-binding proteins have been linked to neurodegenerative disease progression, the physiological role of PLDs and their range of molecular functions are still largely unknown. Here, we show that the PLD of Drosophila Imp, a conserved component of neuronal ribonucleoprotein (RNP) granules, is essential for the developmentally-controlled localization of Imp RNP granules to axons and regulates in vivo axonal remodeling. Furthermore, we demonstrate that Imp PLD restricts, rather than promotes, granule assembly, revealing a novel modulatory function for PLDs in RNP granule homeostasis. Swapping the position of Imp PLD compromises RNP granule dynamic assembly but not transport, suggesting that these two functions are uncoupled. Together, our study uncovers a physiological function for PLDs in the spatio-temporal control of neuronal RNP assemblies.

Indexed as

AnimalsAnimals, Genetically ModifiedAxonal TransportAxonsBrainCell LineCytoplasmic GranulesDrosophila melanogasterDrosophila ProteinsFemaleMicroscopy, FluorescenceModels, AnimalPrionsProtein DomainsRibonucleoproteinsRNA-Binding ProteinsDrosophila ProteinsImp protein, DrosophilaPrionsRibonucleoproteinsRNA-Binding Proteins

Identifiers

PMID31197139
PMCPMC6565635
OpenAlexW2950016845

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.