Evidence map›Paper›PMID 35102251›Full record

ArticleOncogene2022

The ubiquitin E3 ligase ARIH1 regulates hnRNP E1 protein stability, EMT and breast cancer progression.

Breege V Howley, Bidyut Mohanty, Annamarie Dalton, Simon Grelet, Joseph Karam, Toros Dincman, Philip H Howe

Open access · hybridAbstract read
In one paragraph

Article in Oncogene, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 31 citations in OpenAlex.

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  18. Functions and mechanisms of RNA mInternational journal of oncology · 2024
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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 1 institution in 1 country.

Breege V HowleyDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Bidyut MohantyDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Annamarie DaltonDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Simon GreletDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.
Joseph KaramDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA.ORCID http://orcid.org/0000-0002-4536-7362
Toros DincmanDepartment of Medicine, Medical University of South Carolina, Charleston, SC, USA.
Philip H HoweDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, USA. howep@musc.edu.ORCID http://orcid.org/0000-0002-1358-1313
Medical University of South Carolina · US

Funding

South Carolina Clinical & Translational Research Institute (SCTR)UL1TR001450 · NCATS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI BRADY, KATHLEEN T., FLUME, PATRICK A · 2015 to 2024
$41.1M
South Carolina Clinical & Translational Research Institute (SCTR)KL2TR001452 · NCATS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI MCRAE-CLARK, AIMEE L · 2015 to 2024
$5.9M
TGF-regulated EMTR01CA154663 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI Philip H Howe · 2011 to 2026
$5.1M
NCATS NIH HHS KL2 TR001452NCATS NIH HHS UL1 TR001450NCI NIH HHS R01 CA154663
6 · The paper itself

Abstract

The epithelial to mesenchymal transition (EMT), a process that is aberrantly activated in cancer and facilitates metastasis to distant organs, requires coordinated transcriptional and post-transcriptional control of gene expression. The tumor-suppressive RNA binding protein, hnRNP-E1, regulates splicing and translation of EMT-associated transcripts and it is thought that it plays a major role in the control of epithelial cell plasticity during cancer progression. We have utilized yeast 2 hybrid screening to identify novel hnRNP-E1 interactors that play a role in regulating hnRNP-E1; this approach led to the identification of the E3 ubiquitin ligase ARIH1. Here, we demonstrate that hnRNP-E1 protein stability is increased upon ARIH1 silencing, whereas, overexpression of ARIH1 leads to a reduction in hnRNP-E1. Reduced ubiquitination of hnRNP-E1 detected in ARIH1 knockdown (KD) cells compared to control suggests a role for ARIH1 in hnRNP-E1 degradation. The identification of hnRNP-E1 as a candidate substrate of ARIH1 led to the characterization of a novel function for this ubiquitin ligase in EMT induction and cancer progression. We demonstrate a delayed induction of EMT and reduced invasion in mammary epithelial cells silenced for ARIH1. Conversely, ARIH1 overexpression promoted EMT induction and invasion. ARIH1 silencing in breast cancer cells significantly attenuated cancer cell stemness in vitro and tumor formation in vivo. Finally, we utilized miniTurboID proximity labeling to identify novel ARIH1 interactors that may contribute to ARIH1's function in EMT induction and cancer progression.

Indexed as

Breast NeoplasmsEpithelial-Mesenchymal TransitionCell Line, TumorFemaleHeterogeneous-Nuclear RibonucleoproteinsHumansProtein StabilityRNA-Binding ProteinsUbiquitinUbiquitin-Protein LigasesARIH1 protein, humanHeterogeneous-Nuclear RibonucleoproteinsRNA-Binding ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID35102251
PMCPMC8933277
OpenAlexW4210444779

What OpenQuestion holds

Textmetadata
LicenceTDM
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.