Evidence map›Paper›PMID 20086104›Full record

ArticleMolecular and cellular biology2010

Identification and analysis of the interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae.

Yuriko Harigaya, Brittnee N Jones, Denise Muhlrad, John D Gross, Roy Parker

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  12. Article
  13. Article
  14. Numerous interactions act redundantly to assemble a tunable size of P bodies inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. A unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Article
  18. New insights into decapping enzymes and selective mRNA decay.Wiley interdisciplinary reviews. RNA · 2017
    Review
  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

5 authors at 2 institutions in 1 country.

Yuriko HarigayaDepartment of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, Tucson, Arizona 85721-0106, USA.
Brittnee N Jones
Denise Muhlrad
John D Gross
Roy Parker
University of Arizona · USUniversity of California, San Francisco · US

Funding

Structure and Function of the Decapping Enzyme ComplexR01GM078360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GROSS, JOHN D · 2009 to 2018
$2.5M
NIGMS NIH HHS R01 GM078360
6 · The paper itself

Abstract

Cap hydrolysis is a critical control point in the life of eukaryotic mRNAs and is catalyzed by the evolutionarily conserved Dcp1-Dcp2 complex. In Saccharomyces cerevisiae, decapping is modulated by several factors, including the Lsm family protein Edc3, which directly binds to Dcp2. We show that Edc3 binding to Dcp2 is mediated by a short peptide sequence located C terminal to the catalytic domain of Dcp2. This sequence is required for Edc3 to stimulate decapping activity of Dcp2 in vitro, for Dcp2 to efficiently accumulate in P-bodies, and for efficient degradation of the RPS28B mRNA, whose decay is enhanced by Edc3. In contrast, degradation of YRA1 pre-mRNA, another Edc3-regulated transcript, occurs independently from this region, suggesting that the effect of Edc3 on YRA1 is independent of its interaction with Dcp2. Deletion of the sequence also results in a subtle but significant defect in turnover of the MFA2pG reporter transcript, which is not affected by deletion of EDC3, suggesting that the region affects some other aspect of Dcp2 function in addition to binding Edc3. These results raise a model for Dcp2 recruitment to specific mRNAs where regions outside the catalytic core promote the formation of different complexes involved in mRNA decapping.

Indexed as

Amino AcidsAmino Acid SequenceConserved SequenceCytoplasmic StructuresEndoribonucleasesMolecular Sequence DataMutationNuclear ProteinsProtein BindingRibosomal ProteinsRNA-Binding ProteinsRNA PrecursorsRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino AcidsDCP2 protein, S cerevisiaeEDC3 protein, S cerevisiaeEndoribonucleasesNuclear ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA PrecursorsRPS28B protein, S cerevisiaeSaccharomyces cerevisiae ProteinsYRA1 protein, S cerevisiae

Identifiers

PMID20086104
PMCPMC2832485
OpenAlexW2170152673

What OpenQuestion holds

Textmetadata
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.