Evidence map›Paper›PMID 40884268›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

Hypoxia-Induced PRMT1 Lactylation Drives Vimentin Arginine Asymmetric Dimethylation in Tumor Metastasis.

Jia Zhou, Shuying Qiu, Xia Yang, Yan Wu, Xinxia Yao, Hangqi Hu, Jingfeng Luo, Chandra Sugiarto Wijaya, Lingfeng Ma, Xiaojun Long and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

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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

17 authors.

Jia ZhouDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.ORCID https://orcid.org/0000-0002-6277-6491
Shuying QiuDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Xia YangDepartment of pathology, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Yan WuDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Xinxia YaoDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Hangqi HuDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Jingfeng LuoDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Chandra Sugiarto WijayaDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Lingfeng MaDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Xiaojun LongDepartment of Colorectal Surgery, Key Laboratory of Biological Treatment of Zhejiang Province, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Lingna XuDepartment of Colorectal Surgery, Key Laboratory of Biological Treatment of Zhejiang Province, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Jinquan LiuDepartment of Hepatobiliary and Pancreatic Surgery and Zhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310029, China.
Chaoqun WangDepartment of Pathology, Affiliated Dongyang Hospital of Wenzhou Medical University, Dongyang, Zhejiang, 322100, China.
Yibin PanDepartment of Obstetrics and Gynecology, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Xiaona ChenDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Hongchuan JinDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.
Xian WangDepartment of Medical Oncology, Cancer Center of Zhejiang University, Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310016, China.

Funding

National Natural Science Foundation of China 82473486Natural Science Foundation of Zhejiang Province LQ23H160040Natural Science Foundation of Zhejiang Province LY24H160021
6 · The paper itself

Abstract

Metastasis contributes to around 90% of cancer mortality, but effective strategies to disrupt metastatic cascades remain elusive. Hypoxia-driven epithelial-mesenchymal transition (EMT) promotes cancer cell spread, yet the post-translational mechanisms governing cytoskeletal reprogramming here remain incompletely defined. This study reports a hypoxia-inducible post-translational modification cascade: under hypoxia, protein arginine methyltransferase 1 (PRMT1) is lactylated at evolutionarily conserved residues K134/K145, enhancing its methyltransferase activity to catalyze the asymmetric dimethylation (aDMA) of vimentin at R64. This modification drives vimentin filament assembly, cytoskeletal remodeling, and metastasis in preclinical models. shPRMT1 or vimentin R64K mutation (methylation-deficient) abrogates hypoxia-enhanced migration in vitro and metastasis in vivo. Hypoxia reduces the protein levels of HDAC8 (PRMT1's delactylase), boosting PRMT1 lactylation. PRMT1 K134R/K145R mutants (lactylation - deficient) lose the ability to bind vimentin and fail to rescue filament formation. In triple-negative breast cancer (TNBC), vimentin R64 aDMA levels correlate with advanced tumor stage and poor patient survival. PRMT1 inhibitor MS023 reduces xenograft metastasis with low toxicity. These findings establish a hypoxia-PRMT1-vimentin axis, identifying vimentin R64 aDMA as a metastatic regulator. Inhibiting PRMT1 represents a promising anti-metastasis strategy.

Indexed as

ArginineProtein-Arginine N-MethyltransferasesRepressor ProteinsVimentinAnimalsCell Line, TumorEpithelial-Mesenchymal TransitionFemaleHumansMethylationMiceNeoplasm MetastasisProtein Processing, Post-TranslationalArgininePRMT1 protein, humanProtein-Arginine N-MethyltransferasesRepressor ProteinsVimentinVIM protein, humanarginine methylationcancer metastasishypoxialactylationPRMT1vimentin

Identifiers

PMID40884268
PMCPMC12591124

What Socratic holds

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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.