Evidence map›Paper›PMID 24368805›Full record

ArticleThe Journal of cell biology2013

In vitro reconstitution of an mRNA-transport complex reveals mechanisms of assembly and motor activation.

Roland G Heym, Dennis Zimmermann, Franziska T Edelmann, Lars Israel, Zeynep Ökten, David R Kovar, Dierk Niessing

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. 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
1.3field-weighted citation impact, top 20% 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, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Myosin-Driven Intracellular Transport.Cold Spring Harbor perspectives in biology · 2018
    Review
  10. Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018
    Review
  11. Article
  12. Review
  13. Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

7 authors at 4 institutions in 3 countries.

Roland G HeymInstitute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, 85764 Neuherberg, Germany.
Dennis Zimmermann
Franziska T Edelmann
Lars Israel
Zeynep Ökten
David R Kovar
Dierk Niessing
Gene Therapy Laboratory · FRHelmholtz Zentrum München · DEUniversity of Chicago · USLudwig-Maximilians-Universität München · DE

Funding

Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
Intramural NIH HHSNCATS NIH HHS UL1 TR000430NCATS NIH HHS UL1TR000430
6 · The paper itself

Abstract

The assembly and composition of ribonucleic acid (RNA)-transporting particles for asymmetric messenger RNA (mRNA) localization is not well understood. During mitosis of budding yeast, the Swi5p-dependent HO expression (SHE) complex transports a set of mRNAs into the daughter cell. We recombinantly reconstituted the core SHE complex and assessed its properties. The cytoplasmic precomplex contains only one motor and is unable to support continuous transport. However, a defined interaction with a second, RNA-bound precomplex after its nuclear export dimerizes the motor and activates processive RNA transport. The run length observed in vitro is compatible with long-distance transport in vivo. Surprisingly, SHE complexes that either contain or lack RNA cargo show similar motility properties, demonstrating that the RNA-binding protein and not its cargo activates motility. We further show that SHE complexes have a defined size but multimerize into variable particles upon binding of RNAs with multiple localization elements. Based on these findings, we provide an estimate of number, size, and composition of such multimeric SHE particles in the cell.

Indexed as

Cell Cycle ProteinsCytoskeletal ProteinsDimerizationMyosin Heavy ChainsMyosin Type VRNA-Binding ProteinsRNA, MessengerRNA TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsCell Cycle ProteinsCytoskeletal ProteinsMyo4 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSHE2 protein, S cerevisiaeSHE4 protein, S cerevisiaeSWI5 protein, S cerevisiaeTranscription Factors

Identifiers

PMID24368805
PMCPMC3871432
OpenAlexW2084695600

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.