Evidence map›Paper›PMID 27941885›Full record

ArticleOncogene2017

DBC2/RhoBTB2 functions as a tumor suppressor protein via Musashi-2 ubiquitination in breast cancer.

Y M Choi, K B Kim, J H Lee, Y K Chun, I S An, S An, S Bae

Open access · hybridAbstract read
In one paragraph

Article in Oncogene, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Isoform-Specific Localization Diversifies Human MSI2 Function.bioRxiv : the preprint server for biology · 2026
    Article
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  9. Variants inFrontiers in pediatrics · 2024
    Review
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  12. Review
  13. Genotype-phenotype correlations in RHOBTB2-associated neurodevelopmental disorders.Genetics in medicine : official journal of the American College of Medical Genetics · 2023
    Article
  14. Article
  15. Article
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  17. Article
  18. Review
  19. [Advances in research of Musashi2 in solid tumors].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022
    Review
  20. 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

7 authors at 3 institutions in 1 country.

Y M ChoiKU Center for Integrated Science and Technology, Konkuk University, Seoul, South Korea.
K B KimKorea Institute of Dermatological Sciences, 2nd Enterprise Research Building, Chungcheongbuk-do, South Korea.
J H LeeLaboratory of Molecular Oncology, Cheil General Hospital and Women's Healthcare Center, Dankook University, College of Medicine, Seoul, South Korea.
Y K ChunDepartment of Pathology, Cheil General Hospital and Women's Healthcare Center, Dankook University, College of Medicine, Seoul, South Korea.
I S AnKorea Institute of Dermatological Sciences, 2nd Enterprise Research Building, Chungcheongbuk-do, South Korea.
S AnKU Center for Integrated Science and Technology, Konkuk University, Seoul, South Korea.
S BaeKU Center for Integrated Science and Technology, Konkuk University, Seoul, South Korea.
Konkuk University · KRCheil General Hospital and Women's Healthcare Center · KRDankook University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gene encoding 'deleted in breast cancer 2' (DBC2), also referred to as RHOBTB2 (Rho-related BTB domain-containing protein 2), is classified as a tumor suppressor gene. DBC2 is a substrate-specific adaptor protein for a novel class of Cullin-3 (CUL3)-based E3 ubiquitin ligases; however, it is unclear if the substrate adaptor function of DBC2 is required for its tumor suppressor activity. Furthermore, the key substrates of DBC2-mediated ubiquitination have yet to be identified. In the present study, we established a genome-wide human cDNA library-based in vitro ubiquitination target screening assay and identified Musashi-2 (MSI2) as a novel ubiquitination target protein of DBC2. MSI2 directly interacted with DBC2, and this interaction promoted MSI2 polyubiquitination and proteasomal degradation in breast cancer cells. Overexpression and knockdown experiments demonstrated that DBC2 suppressed MSI2-associated oncogenic functions and induced apoptosis. Immunohistochemistry analysis of a breast cancer tissue microarray revealed that DBC2 and MSI2 protein levels are inversely correlated in both normal breast tissues and breast cancer tissues. Taken together, these findings provide evidence that DBC2 suppresses tumorigenesis in breast cancer by ubiquitinating MSI2.

Indexed as

AdultAgedBiomarkers, TumorBreast NeoplasmsCell Line, TumorFemaleGene Knockdown TechniquesGTP-Binding ProteinsHumansMiddle AgedNeoplasm GradingProteasome Endopeptidase ComplexProtein BindingProtein StabilityProteolysisRNA-Binding ProteinsBiomarkers, TumorGTP-Binding ProteinsMSI2 protein, humanProteasome Endopeptidase ComplexRHOBTB2 protein, humanRNA-Binding ProteinsTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID27941885
PMCPMC5442418
OpenAlexW2563105066

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.