Evidence map›Paper›PMID 23150776›Full record

ArticleScientific reports2012

Dishevelled3 is a novel arginine methyl transferase substrate.

Rama Kamesh Bikkavilli, Sreedevi Avasarala, Michelle Vanscoyk, Marybeth Sechler, Nicole Kelley, Craig C Malbon, Robert A Winn

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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  5. The Role of Protein Arginine Methyltransferases in DNA Damage Response.International journal of molecular sciences · 2022
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  18. Asymmetric arginine dimethylation of RelA provides a repressive mark to modulate TNFα/NF-κB response.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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

7 authors at 3 institutions in 1 country.

Rama Kamesh BikkavilliDivision of Pulmonary Sciences and Critical Care, School of Medicine, Anschutz Medical Campus, University of Colorado Health Sciences Center, Aurora, Colorado 80045, USA. kamesh.bikkavilli@ucdenver.edu
Sreedevi Avasarala
Michelle Vanscoyk
Marybeth Sechler
Nicole Kelley
Craig C Malbon
Robert A Winn
University of Colorado Health · USUniversity of Colorado Anschutz Medical Campus · USStony Brook University · US

Funding

REGULATION OF HORMONE-SENSITIVE EFFECTOR SYSTEMSR01DK030111 · NIDDK · STATE UNIVERSITY NEW YORK STONY BROOK · PI MALBON, CRAIG C · 1986 to 2010
$3.5M
Role of the noncanonical WNT pathway in non-small cell lung cancerR01CA138528 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI WINN, ROBERT A. · 2010 to 2014
$1.4M
Wnt 7a and Its Role in EMT and Lung Cancer MetastasisR21CA153268 · NCI · UNIVERSITY OF COLORADO DENVER · PI WINN, ROBERT A. · 2010 to 2011
$270k
NCI NIH HHS 5R21CA153268-02NCI NIH HHS R01 CA138528NCI NIH HHS R01CA1385282522717NCI NIH HHS R21 CA153268NIDDK NIH HHS DK30111NIDDK NIH HHS R01 DK030111
6 · The paper itself

Abstract

Dishevelled, a phosphoprotein scaffold, is a central component in all the Wnt-sensitive signaling pathways. In the present study, we report that Dishevelled is post-translationally modified, both in vitro and in vivo, via arginine methylation. We also show protein arginine methyl transferases 1 and 7 as the key enzymes catalyzing Dishevelled methylation. Interestingly, Wnt3a stimulation of F9 teratocarcinoma cells results in reduced Dishevelled methylation. Similarly, the methylation-deficient mutant of Dishevelled, R271K, displayed spontaneous membrane localization and robust activation of Wnt signaling; suggesting that differential methylation of Dishevelled plays an important role in Wnt signaling. Thus arginine methylation is shown to be an important switch in regulation of Dishevelled function and Wnt signaling.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsArginineCell LineCell MembraneDishevelled ProteinsDrosophilaDrosophila ProteinsHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMethylationMiceMolecular Sequence DataMutationAdaptor Proteins, Signal TransducingArginineDishevelled ProteinsDrosophila Proteinsdsh protein, DrosophilaDVL3 protein, humanDvl3 protein, mouseIntracellular Signaling Peptides and ProteinsPhosphoproteinsPRMT1 protein, humanPRMT2 protein, humanPRMT7 protein, humanProtein-Arginine N-MethyltransferasesRepressor ProteinsWnt Proteins

Identifiers

PMID23150776
PMCPMC3496165
OpenAlexW2088920401

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.