Evidence map›Paper›PMID 25361079›Full record

ArticleCell death and differentiation2015

Involvement of RARRES3 in the regulation of Wnt proteins acylation and signaling activities in human breast cancer cells.

T-H Hsu, S-Y Jiang, W-L Chang, W-L Chan, R L Eckert, T M Scharadin, T-C Chang

Erratum issuedOpen access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death and differentiation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

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  9. Forward Genetics in Apicomplexa Biology: The Host Side of the Story.Frontiers in cellular and infection microbiology · 2022
    Review
  10. Article
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  16. Article
  17. Palmitoylation: a proteinNPJ breast cancer · 2016
    Review
  18. Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

T-H Hsu1] Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan, ROC [2] Genomics Research Center, Academia Sinica, Taipei, Taiwan, ROC.
S-Y JiangDepartment of Medical Education and Research, The Buddhist Tzu Chi General Hospital, Taipei, Taiwan, ROC.
W-L Chang
W-L ChanDepartment of Pharmacy, National Defense Medical Center, Taipei, Taiwan, ROC.
R L Eckert1] Department of Biochemistry and Molecular Biology, School of Medicine, University of Maryland, Baltimore, MD, USA [2] Department of Dermatology, School of Medicine, University of Maryland, Baltimore, MD, USA [3] Department of Obstetrics and Gynecology and Reproductive Sciences, School of Medicine, University of Maryland, Baltimore, MD, USA.
T M ScharadinDepartment of Biochemistry and Molecular Biology, School of Medicine, University of Maryland, Baltimore, MD, USA.
T-C Chang1] Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan, ROC [2] Department of Biotechnology, Asia University, Taichung, Taiwan, ROC [3] Graduate Institute of Basic Medical Science, China Medical University, Taichung, Taiwan, ROC [4] Department of Biochemistry, National Defense Medical Center, Taipei, Taiwan, ROC.
National Defense Medical Center · TWUniversity of Maryland, Baltimore · USAsia University · TWBuddhist Tzu Chi General Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Wnt/β-catenin signaling pathway has emerged as a key regulator of complex biological processes, such as embryonic development, cell proliferation, cell fate decision and tumorigenesis. Recent studies have shown that the deregulation of Wnt/β-catenin signaling is frequently observed and leads to abnormal cell growth in human breast cancer cells. In this study, we identified a novel regulatory mechanism of Wnt/β-catenin signaling through RARRES3 that targets and modulates the acylation status of Wnt proteins and co-receptor low-density lipoprotein receptor-related protein 6, resulting in the suppression of epithelial-mesenchymal transition and cancer stem cell properties. Mutation of the conserved active site residues of RARRES3 indicates that RARRES3 serves as an acyl protein thioesterase that tethers its target proteins and modulates their acylation status. Furthermore, the functions of p53 in cell proliferation and Wnt/β-catenin signaling are significantly associated with the induction of RARRES3. Thus our findings provide a new insight into the molecular link between p53, protein acylation and Wnt/β-catenin signaling whereby RARRES3 plays a pivotal role in modulating the acylation status of signaling proteins.

Indexed as

Cell ProliferationEpithelial-Mesenchymal TransitionWnt Signaling PathwayAcylationBreast NeoplasmsFemaleHumansMCF-7 CellsReceptors, Retinoic AcidTumor Suppressor Protein p53PLAAT4 protein, humanReceptors, Retinoic AcidTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID25361079
PMCPMC4392077
OpenAlexW4229779114

What OpenQuestion holds

Textmetadata
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.