Evidence map›Paper›PMID 24504254›Full record

ArticleG3 (Bethesda, Md.)2014

Edc3 function in yeast and mammals is modulated by interaction with NAD-related compounds.

Robert W Walters, Igor A Shumilin, Je-Hyun Yoon, Wladek Minor, Roy Parker

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Eukaryotic RNA 5'-End NADTrends in cell biology · 2018
    Review
  4. Metabolic influences on RNA biology and translation.Critical reviews in biochemistry and molecular biology · 2017
    Review
  5. Identification of NAD+ capped mRNAs in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Article
  7. 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 4 institutions in 1 country.

Robert W WaltersDepartment Chemistry and Biochemistry, University of Colorado, Boulder, Colorado.
Igor A Shumilin
Je-Hyun Yoon
Wladek Minor
Roy Parker
University of Virginia · USHoward Hughes Medical Institute · USNational Institutes of Health · USUniversity of Arizona · US

Funding

Stress Granules in Yeast and MammalsR01GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 1991 to 2021
$3.3M
mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
Howard Hughes Medical InstituteNIGMS NIH HHS GM45443NIGMS NIH HHS R01 GM045443NIGMS NIH HHS R37 GM045443
6 · The paper itself

Abstract

The control of mRNA translation and degradation is mediated in part by a set of proteins that can inhibit translation and promote decapping, as well as function in the assembly of cytoplasmic mRNP granules referred to as processing bodies (P-bodies). The conserved enhancer of mRNA decapping 3 (Edc3) protein functions to promote both decapping and P-body assembly. Crystal structures of the YjeF_N domain in hEdc3 identified a putative binding site for a small molecule. Structure modeling of the human Edc3 Yjef_N along with other Yjef_N-containing proteins suggests that this molecule is related to NAD(H). We now show human Edc3 directly binds NADH. We also show that human and yeast Edc3 chemically modify NAD in vitro. Mutations that are predicted to disrupt the binding and/or hydrolysis of an NAD-related molecule by yeast and human Edc3 affect the control of mRNA degradation and/or P-body composition in vivo. This suggests that the interaction of Edc3 with an NAD-related molecule affects its function in the regulation of mRNA translation and degradation and provides a possible mechanism to couple the energetics of the cell to posttranscriptional control. Moreover, this provides a unique example of and lends strength to the postulated connection of metabolites, enzymes, and RNA.

Indexed as

Binding SitesHeLa CellsHumansMolecular Docking SimulationMutationNADProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEDC3 protein, humanEDC3 protein, S cerevisiaeNADRibonucleoproteins, Small NuclearRNA, MessengerSaccharomyces cerevisiae ProteinsdecappingEdc3mRNA decayP bodies

Identifiers

PMID24504254
PMCPMC4059234
OpenAlexW2048609725

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.