Evidence map›Paper›PMID 31700102›Full record

ArticleScientific reports2019

Acetylation of conserved DVL-1 lysines regulates its nuclear translocation and binding to gene promoters in triple-negative breast cancer.

Monica Sharma, Deborah Molehin, Isabel Castro-Piedras, Edgar G Martinez, Kevin Pruitt

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  7. Frizzled receptors: gatekeepers of Wnt signaling in development and disease.Frontiers in cell and developmental biology · 2025
    Review
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  15. Decoding the Role of DVL1 in Intracranial Meningioma.International journal of molecular sciences · 2021
    Article
  16. Article
  17. Article
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  19. Article
  20. Regulation of aromatase in cancer.Molecular and cellular biochemistry · 2021
    Review
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.

Monica SharmaDepartment of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Deborah MolehinDepartment of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Isabel Castro-PiedrasDepartment of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Edgar G MartinezDepartment of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Kevin PruittDepartment of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA. kevin.pruitt@ttuhsc.edu.
Texas Tech University · USTexas Tech University Health Sciences Center · US

Funding

Mechanisms of Epigenetic Gene SilencingR01CA155223 · NCI · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI PRUITT, KEVIN · 2011 to 2015
$1.4M
Cancer Prevention and Research Institute of Texas (Cancer Prevention Research Institute of Texas) RR410008NCI NIH HHS R01 CA155223
6 · The paper itself

Abstract

Dishevelled (DVL) proteins are central mediators of the Wnt signalling pathway and are versatile regulators of several cellular processes, yet little is known about their post-translational regulation. Acetylation is a reversible post-translational modification (PTM) which regulates the function of several non-histone proteins involved in tumorigenesis. Since we previously demonstrated that lysine deacetylase, SIRT-1, regulates DVL protein levels and its function, we reasoned that DVL could potentially be a substrate for SIRT-1 mediated deacetylation. To further examine the potential role of multiple families of lysine deacetylases in the post-translational regulation of DVL, we screened for novel acetylation sites using liquid chromatography mass-spectrometry (LC-MS/MS) analysis. Herein, we report 12 DVL-1 lysine residues that show differential acetylation in response to changes in oxygen tension and deacetylase inhibition in triple-negative breast cancer (TNBC). PTMs are well documented to influence protein activity, and cellular localization. We also identify that acetylation of two key lysine residues, K69 and K285, present on the DIX and PDZ domains respectively, promote nuclear over cytoplasmic localization of DVL-1, and influences its promoter binding and regulation of genes implicated in cancer. Collectively, these findings for the first time, uncover acetylation as a novel layer of regulation of DVL-1 proteins.

Indexed as

Promoter Regions, GeneticAcetylationAmino Acid SequenceAromataseBiomarkersCell Line, TumorCell NucleusDishevelled ProteinsDNA-Binding ProteinsFemaleGene Expression Regulation, NeoplasticHumansLysineModels, BiologicalOxygenProtein BindingAromataseBiomarkersCYP19A1 protein, humanDishevelled ProteinsDNA-Binding ProteinsDVL1 protein, humanDVL3 protein, humanLysineOxygen

Identifiers

PMID31700102
PMCPMC6838061
OpenAlexW2987536484

What OpenQuestion holds

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LicenceCC BY
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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.