Evidence map›Paper›PMID 31699982›Full record

ArticleNature communications2019

Insights into the assembly and architecture of a Staufen-mediated mRNA decay (SMD)-competent mRNP.

Manjeera Gowravaram, Juliane Schwarz, Sana K Khilji, Henning Urlaub, Sutapa Chakrabarti

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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Metamorphosis and lncRNAs: A Close Relationship.Genesis (New York, N.Y. : 2000) · 2026
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  19. Emerging Roles of RNA-Binding Proteins in Neurodevelopment.Journal of developmental biology · 2022
    Review
  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

5 authors at 3 institutions in 1 country.

Manjeera GowravaramInstitute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 6, 14195, Berlin, Germany.
Juliane SchwarzBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Goettingen, Germany.
Sana K KhiljiInstitute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 6, 14195, Berlin, Germany.
Henning UrlaubBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Goettingen, Germany.
Sutapa ChakrabartiInstitute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse 6, 14195, Berlin, Germany. chakraba@zedat.fu-berlin.de.ORCID http://orcid.org/0000-0002-9877-173X
Freie Universität Berlin · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute of Colloids and Interfaces · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mammalian Staufen proteins (Stau1 and Stau2) mediate degradation of mRNA containing complex secondary structures in their 3'-untranslated region (UTR) through a pathway known as Staufen-mediated mRNA decay (SMD). This pathway also involves the RNA helicase UPF1, which is best known for its role in the nonsense-mediated mRNA decay (NMD) pathway. Here we present a biochemical reconstitution of the recruitment and activation of UPF1 in context of the SMD pathway. We demonstrate the involvement of UPF2, a core NMD factor and a known activator of UPF1, in SMD. UPF2 acts as an adaptor between Stau1 and UPF1, stimulates the catalytic activity of UPF1 and plays a central role in the formation of an SMD-competent mRNP. Our study elucidates the molecular mechanisms of SMD and points towards extensive cross-talk between UPF1-mediated mRNA decay pathways in cells.

Indexed as

Cell Line, TumorCytoskeletal ProteinsGene Knockdown TechniquesHumansNonsense Mediated mRNA DecayProtein Structure, QuaternaryProtein Structure, TertiaryRibonucleoproteinsRNA-Binding ProteinsRNA HelicasesRNA, MessengerRNA StabilityTrans-ActivatorsCytoskeletal Proteinsmessenger ribonucleoproteinRibonucleoproteinsRNA-Binding ProteinsRNA HelicasesRNA, MessengerSTAU1 protein, humanTrans-ActivatorsUPF1 protein, humanUPF2 protein, human

Identifiers

PMID31699982
PMCPMC6838198
OpenAlexW2985297330

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.