Evidence map›Paper›PMID 34026434›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2021

PRMT5 Enables Robust STAT3 Activation via Arginine Symmetric Dimethylation of SMAD7.

Congcong Cai, Shuchen Gu, Yi Yu, Yezhang Zhu, HanChenxi Zhang, Bo Yuan, Li Shen, Bing Yang, Xin-Hua Feng

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

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  15. A biomechanical view of epigenetic tumor regulation.Journal of biological physics · 2023
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  20. PRMT5 Enables Robust STAT3 Activation via Arginine Symmetric Dimethylation of SMAD7.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
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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

9 authors at 2 institutions in 1 country.

Congcong CaiThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Shuchen GuThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Yi YuThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Yezhang ZhuThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
HanChenxi ZhangThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Bo YuanThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Li ShenThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Bing YangThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.
Xin-Hua FengThe MOE Key Laboratory of Biosystems Homeostasis & Protection and Innovation Center for Cell Signaling Network, Life Sciences Institute Zhejiang University Hangzhou Zhejiang 310058 China.ORCID 0000-0002-4418-0811
Zhejiang University · CNZhejiang Cancer Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferase 5 (PRMT5) is the type II arginine methyltransferase that catalyzes the mono- and symmetrical dimethylation of protein substrates at the arginine residues. Emerging evidence reveals that PRMT5 is involved in the regulation of tumor cell proliferation and cancer development. However, the exact role of PRMT5 in human lung cancer cell proliferation and the underlying molecular mechanism remain largely elusive. Here, it is shown that PRMT5 promotes lung cancer cell proliferation through the Smad7-STAT3 axis. Depletion or inhibition of PRMT5 dramatically dampens STAT3 activation and thus suppresses the proliferation of human lung cancer cells. Furthermore, depletion of Smad7 blocks PRMT5-mediated STAT3 activation. Mechanistically, PRMT5 binds to and methylates Smad7 on Arg-57, enhances Smad7 binding to IL-6 co-receptor gp130, and consequently ensures robust STAT3 activation. The findings position PRMT5 as a critical regulator of STAT3 activation, and suggest it as a potential therapeutic target for the treatment of human lung cancer.

Indexed as

ArginineCell Line, TumorCell ProliferationHumansLung NeoplasmsMethylationPrognosisProtein-Arginine N-MethyltransferasesSmad7 ProteinSTAT3 Transcription FactorArgininePRMT5 protein, humanProtein-Arginine N-MethyltransferasesSmad7 ProteinSMAD7 protein, humanSTAT3 protein, humanSTAT3 Transcription FactormethylationmigrationPRMT5proliferationSmad7STAT3

Identifiers

PMID34026434
PMCPMC8132155
OpenAlexW3132897663

What OpenQuestion holds

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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.