Evidence map›Paper›PMID 19454603›Full record

ArticleNucleic acids research2009

Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.

Anne E McBride, Ana K Conboy, Shanique P Brown, Chaiyaboot Ariyachet, Kate L Rutledge

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  14. Keeping mRNPs in check during assembly and nuclear export.Nature reviews. Molecular cell biology · 2011
    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 1 institution in 1 country.

Anne E McBrideDepartment of Biology, Bowdoin College, Brunswick, ME 04011, USA. amcbride@bowdoin.edu
Ana K Conboy
Shanique P Brown
Chaiyaboot Ariyachet
Kate L Rutledge
Bowdoin College · US

Funding

WNT SIGNALING IN THE DEVELOPING GASTROINTESTINAL TRACTP20RR016463 · NCRR · MOUNT DESERT ISLAND BIOLOGICAL LAB · PI WRAY, CHRISTOPHER C · 2001 to 2011
$41.0M
Howard Hughes Medical InstituteNCRR NIH HHS P20 RR-016463NCRR NIH HHS P20 RR016463
6 · The paper itself

Abstract

The discovery of roles for arginine methylation in intracellular transport and mRNA splicing has focused attention on the methylated arginine-glycine (RG)-rich domains found in many eukaryotic RNA-binding proteins. Sequence similarity among these highly repetitive RG domains, combined with interactions between RG-rich proteins, raises the question of whether these regions are general interaction motifs or whether there is specificity within these domains. Using the essential Saccharomyces cerevisiae mRNA-binding protein Npl3 (ScNpl3) as a model system, we first tested the importance of the RG domain for protein function. While Npl3 lacking the RG domain could not support growth of cells lacking Npl3, surprisingly, expression of the RG domain alone supported partial growth of these cells. To address the specificity of this domain, we created chimeric forms of ScNpl3 with RG-rich domains of S. cerevisiae nucleolar proteins, Gar1 and Nop1 (ScGar1, ScNop1), or of the Candida albicans Npl3 ortholog (CaNpl3). Whereas the CaNpl3 RG chimeric protein retained nearly wild-type function in S. cerevisiae, the ScGar1 and ScNop1 RG domains significantly reduced Npl3 function and self-association, indicating RG domain specificity. Nuclear localization of Npl3 also requires specific RG sequences, yet heterologous RG domains allow similar modulation of Npl3 transport by arginine methylation.

Indexed as

ArginineGlycineNuclear ProteinsProtein Structure, TertiaryRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSequence DeletionArginineGlycineNPL3 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19454603
PMCPMC2715232
OpenAlexW2154524095

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.