Evidence map›Paper›PMID 27183195›Full record

ArticleNature structural & molecular biology2016

Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation.

Eugene Valkov, Sowndarya Muthukumar, Chung-Te Chang, Stefanie Jonas, Oliver Weichenrieder, Elisa Izaurralde

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Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Dcp2 C-terminaleLife · 2022
    Article
  14. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  15. Article
  16. Messenger RNA 5' NADDevelopmental cell · 2021
    Article
  17. Article
  18. Article
  19. 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

6 authors at 1 institution in 1 country.

Eugene ValkovDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0002-3721-1739
Sowndarya MuthukumarDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0002-9110-722X
Chung-Te ChangDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Stefanie JonasDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Oliver WeichenriederDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0001-5818-6248
Elisa IzaurraldeDepartment of Biochemistry, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0001-7365-2649
Max Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The removal of the mRNA 5' cap (decapping) by Dcp2 shuts down translation and commits mRNA to full degradation. Dcp2 activity is enhanced by activator proteins such as Dcp1 and Edc1. However, owing to conformational flexibility, the active conformation of Dcp2 and the mechanism of decapping activation have remained unknown. Here, we report a 1.6-Å-resolution crystal structure of the Schizosaccharomyces pombe Dcp2-Dcp1 heterodimer in an unprecedented conformation that is tied together by an intrinsically disordered peptide from Edc1. In this ternary complex, an unforeseen rotation of the Dcp2 catalytic domain allows residues from both Dcp2 and Dcp1 to cooperate in RNA binding, thus explaining decapping activation by increased substrate affinity. The architecture of the Dcp2-Dcp1-Edc1 complex provides a rationale for the conservation of a sequence motif in Edc1 that is also present in unrelated decapping activators, thus indicating that the presently described mechanism of decapping activation is evolutionarily conserved.

Indexed as

Catalytic DomainCrystallography, X-RayPeptidesProtein ConformationProtein MultimerizationSchizosaccharomycesSchizosaccharomyces pombe ProteinsDcp1 protein, S pombeDcp2 protein, S pombePeptidesSchizosaccharomyces pombe Proteins

Identifiers

PMID27183195
OpenAlexW2399190924

What OpenQuestion holds

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Read underepoch 390

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.