Evidence map›Paper›PMID 18086885›Full record

ArticleMolecular and cellular biology2008

Pat1 contains distinct functional domains that promote P-body assembly and activation of decapping.

Guy R Pilkington, Roy Parker

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

69 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  12. Article
  13. Article
  14. Pat1 activates late steps in mRNA decay by multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  18. Article
  19. Control of mRNA decapping by autoinhibition.Nucleic acids research · 2018
    Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Guy R PilkingtonDepartment of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, 1007 E. Lowell St., Tucson, AZ 85721-0206, USA.
Roy Parker
Howard Hughes Medical Institute · USUniversity of Arizona · US

Funding

mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
NIGMS NIH HHS R37 GM045443NIGMS NIH HHS R37 GM45443
6 · The paper itself

Abstract

The control of mRNA degradation and translation are important aspects of gene regulation. Recent results suggest that translation repression and mRNA decapping can be intertwined and involve the formation of a quiescent mRNP, which can accumulate in cytoplasmic foci referred to as P bodies. The Pat1 protein is a key component of this complex and an important activator of decapping, yet little is known about its function. In this work, we analyze Pat1 in Saccharomyces cerevisiae function by deletion and functional analyses. Our results identify two primary functional domains in Pat1: one promoting translation repression and P-body assembly and a second domain promoting mRNA decapping after assembly of the mRNA into a P-body mRNP. In addition, we provide evidence that Pat1 binds RNA and has numerous domain-specific interactions with mRNA decapping factors. These results indicate that Pat1 is an RNA binding protein and a multidomain protein that functions at multiple stages in the process of translation repression and mRNA decapping.

Indexed as

Amino AcidsCytoplasmic StructuresDNA-Binding ProteinsGene DeletionGreen Fluorescent ProteinsModels, BiologicalProtein BindingProtein BiosynthesisProtein Structure, TertiaryRecombinant Fusion ProteinsRNA-Binding ProteinsRNA CapsRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipAmino AcidsDNA-Binding ProteinsGreen Fluorescent ProteinsPAT1 protein, S cerevisiaeRecombinant Fusion ProteinsRNA-Binding ProteinsRNA CapsRNA, FungalSaccharomyces cerevisiae Proteins

Identifiers

PMID18086885
PMCPMC2258743
OpenAlexW2150104695

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.