Evidence map›Paper›PMID 39665584›Full record

ArticleThe Biochemical journal2025

The PRL2 phosphatase up-regulates miR-21 through activation of the JAK2/STAT3 pathway to down-regulate the PTEN tumor suppressor.

Qinglin Li, Yunpeng Bai, Sarah M Cavender, Yiming Miao, Frederick Nguele Meke, Emily L Lasse-Opsahl, Peipei Zhu, Gina M Doody, W Andy Tao, Zhong-Yin Zhang

Abstract read
In one paragraph

Article in The Biochemical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. 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

10 authors.

Qinglin Li *Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.ORCID 0000-0002-4125-1944
Yunpeng Bai *Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.ORCID 0000-0002-5879-3555
Sarah M CavenderBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.
Yiming MiaoBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.
Frederick Nguele MekeBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.ORCID 0000-0001-8542-0343
Emily L Lasse-OpsahlBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.ORCID 0000-0001-6371-9459
Peipei ZhuDepartment of Biochemistry, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.
Gina M DoodyDivision of Haematology and Immunology, Leeds Institute of Medical Research, University of Leeds, U.K.ORCID 0000-0003-0665-6759
W Andy TaoDepartment of Biochemistry, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.ORCID 0000-0002-5535-5517
Zhong-Yin ZhangBorch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 720 Clinic Drive, West Lafayette, IN 47907, U.S.A.ORCID 0000-0001-5527-7910

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI ANDREW D MESECAR · 1985 to 2026
$43.4M
Structure/Function of Protein Tyrosine PhosphatasesR01CA069202 · NCI · YESHIVA UNIVERSITY · PI Zhong-Yin Zhang · 1996 to 2026
$7.3M
Dissecting signaling pathways and seeking EV phosphoproteins as novel biomarkers for Alzheimer's DiseaseR01AG064250 · NIA · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2024 to 2024
$386k
NCI NIH HHS P30 CA023168NCI NIH HHS R01 CA069202NIA NIH HHS R01 AG064250
6 · The paper itself

Abstract

The phosphatases of regenerating liver (PRLs) are members of the protein tyrosine phosphatase (PTP) superfamily that play pro-oncogenic roles in cell proliferation, migration, and survival. We previously demonstrated that PRLs can post-translationally down-regulate PTEN, a tumor suppressor frequently inactivated in human cancers, by dephosphorylating PTEN at Tyr336, which promotes the NEDD4-mediated PTEN ubiquitination and proteasomal degradation. Here, we report that PRLs can also reduce PTEN expression by up-regulating microRNA-21 (miR-21), which is one of the most frequently overexpressed miRNAs in solid tumors. We observe a broad correlation between PRL and miR-21 levels in multiple human cancers. Mechanistically, PRL2, the most abundant and ubiquitously expressed PRL family member, promotes the JAK2/STAT3 pathway-mediated miR-21 expression by directly dephosphorylating JAK2 at Tyr570. Finally, we confirm that the PRL2-mediated miR-21 expression contributes to its oncogenic potential in breast cancer cells. Our study defines a new functional role of PRL2 in PTEN regulation through a miR-21-dependent post-transcriptional mechanism, in addition to our previously reported NEDD4-dependent post-translational PTEN regulation. Together, these studies further establish the PRLs as negative regulators of PTEN.

Indexed as

Janus Kinase 2MicroRNAsProtein Tyrosine PhosphatasesPTEN PhosphohydrolaseSTAT3 Transcription FactorCell Line, TumorDown-RegulationGene Expression Regulation, NeoplasticHEK293 CellsHumansSignal TransductionUp-RegulationJAK2 protein, humanJanus Kinase 2MicroRNAsMIRN21 microRNA, humanProtein Tyrosine PhosphatasesPTEN PhosphohydrolasePTEN protein, humanPTP4A2 protein, humanSTAT3 protein, humanSTAT3 Transcription FactorJAK2miR-21PRL2PTENSTAT3

Identifiers

PMID39665584
PMCPMC12198624

What Socratic 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 Socratic graph.