Evidence map›Paper›PMID 34733415›Full record

ArticleOncotarget2021

Dishevelled-1 DIX and PDZ domain lysine residues regulate oncogenic Wnt signaling.

Monica Sharma, Isabel Castro-Piedras, Fahmida Rasha, Sabarish Ramachandran, Souad R Sennoune, Kathryn Furr, Sharilyn Almodovar, Vadivel Ganapathy, Matthew B Grisham, Rakhshanda Layeequr Rahman and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2021. 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
1.0field-weighted citation impact, top 25% 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, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Frizzled receptors: gatekeepers of Wnt signaling in development and disease.Frontiers in cell and developmental biology · 2025
    Review
  4. Review
  5. 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

11 authors at 2 institutions in 1 country.

Monica SharmaImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Isabel Castro-PiedrasImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Fahmida RashaImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Sabarish RamachandranCell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Souad R SennouneCell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Kathryn FurrImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Sharilyn AlmodovarImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Vadivel GanapathyCell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Matthew B GrishamImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Rakhshanda Layeequr RahmanDepartment of Surgery, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
Kevin PruittImmunology and Molecular Microbiology, Texas Tech University Health Sciences Center, Lubbock, TX, USA.
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
NCI NIH HHS R01 CA155223
6 · The paper itself

Abstract

DVL proteins are central mediators of the Wnt pathway and relay complex input signals into different branches of the Wnt signaling network. However, molecular mechanism(s) that regulate DVL-mediated relay of Wnt signals still remains unclear. Here, for the first time, we elucidate the functional significance of three DVL-1 lysines (K/Lys) which are subject to post-translational acetylation. We demonstrate that K34 Lys residue in the DIX domain regulates subcellular localization of β-catenin, thereby influencing downstream Wnt target gene expression. Additionally, we show that K69 (DIX domain) and K285 (PDZ domain) regulate binding of DVL-1 to Wnt target gene promoters and modulate expression of Wnt target genes including

Indexed as

chromatin immunoprecipitation (ChIP)dishevelled (DVL)gene expressionlysine residuepost-translational modification

Identifiers

PMID34733415
PMCPMC8555683
OpenAlexW3206884299

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.