Evidence map›Paper›PMID 21526221›Full record

ArticlePLoS biology2011

A cytoplasmic complex mediates specific mRNA recognition and localization in yeast.

Marisa Müller, Roland Gerhard Heym, Andreas Mayer, Katharina Kramer, Maria Schmid, Patrick Cramer, Henning Urlaub, Ralf-Peter Jansen, Dierk Niessing

Abstract read
In one paragraph

Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  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. A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Article
  18. Article
  19. Subcellular mRNA localisation at a glance.Journal of cell science · 2014
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Marisa MüllerInstitute of Structural Biology, Helmholtz Zentrum München-German Research Center for Environmental Health, München, Germany.
Roland Gerhard Heym
Andreas Mayer
Katharina Kramer
Maria Schmid
Patrick Cramer
Henning Urlaub
Ralf-Peter Jansen
Dierk Niessing

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, hundreds of mRNAs are localized by specialized transport complexes. For localization, transcripts are recognized by RNA-binding proteins and incorporated into motor-containing messenger ribonucleoprotein particles (mRNPs). To date, the molecular assembly of such mRNPs is not well understood and most details on cargo specificity remain unresolved. We used ASH1-mRNA transport in yeast to provide a first assessment of where and how localizing mRNAs are specifically recognized and incorporated into mRNPs. By using in vitro-interaction and reconstitution assays, we found that none of the implicated mRNA-binding proteins showed highly specific cargo binding. Instead, we identified the cytoplasmic myosin adapter She3p as additional RNA-binding protein. We further found that only the complex of the RNA-binding proteins She2p and She3p achieves synergistic cargo binding, with an at least 60-fold higher affinity for localizing mRNAs when compared to control RNA. Mutational studies identified a C-terminal RNA-binding fragment of She3p to be important for synergistic RNA binding with She2p. The observed cargo specificity of the ternary complex is considerably higher than previously reported for localizing mRNAs. It suggests that RNA binding for mRNP localization generally exhibits higher selectivity than inferred from previous in vitro data. This conclusion is fully consistent with a large body of in vivo evidence from different organisms. Since the ternary yeast complex only assembles in the cytoplasm, specific mRNA recognition might be limited to the very last steps of mRNP assembly. Remarkably, the mRNA itself triggers the assembly of mature, motor-containing complexes. Our reconstitution of a major portion of the mRNA-transport complex offers new and unexpected insights into the molecular assembly of specific, localization-competent mRNPs and provides an important step forward in our mechanistic understanding of mRNA localization in general.

Indexed as

Amino Acid SequenceCell NucleusCytoplasmInverted Repeat SequencesMolecular Sequence DataMutagenesis, Site-DirectedNucleic Acid ConformationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerRNA TransportASH1 protein, S cerevisiaemessenger ribonucleoproteinPuf6 protein, S cerevisiaeRepressor ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSHE2 protein, S cerevisiaeSHE3 protein, S cerevisiae

Identifiers

PMID21526221
PMCPMC3079584

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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.