Evidence map›Paper›PMID 41344331›Full record

ArticleMolecular cell2025

NAT10 promotes cancer metastasis by modulating p300/CBP activity through chromatin-associated tRNA.

Ruhul Amin, Ngoc-Han Ha, Tinghu Qiu, Ronald Holewinski, Khiem C Lam, Amélie Daugherty-Lopès, Huaitian Liu, Andy D Tran, Maxwell P Lee, Thorkell Andresson and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Functional roles and mechanisms of NAT10-mediated RNA acFrontiers in cell and developmental biology · 2026
    Review
  7. 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

12 authors.

Ruhul AminLaboratory of Cancer Biology and Genetics, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA. Electronic address: ruhul.amin@nih.gov.
Ngoc-Han HaLaboratory of Cancer Biology and Genetics, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Tinghu QiuLaboratory of Cancer Biology and Genetics, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Ronald HolewinskiProtein Characterization Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Khiem C LamInflammatory Cell Dynamics Section, Laboratory of Integrative Cancer Immunology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Amélie Daugherty-LopèsInflammatory Cell Dynamics Section, Laboratory of Integrative Cancer Immunology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Huaitian LiuLaboratory of Human Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Andy D TranConfocal Microscopy Core Facility, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Maxwell P LeeHigh-Dimension Data Analysis Group, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Thorkell AndressonProtein Characterization Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Romina S GoldszmidInflammatory Cell Dynamics Section, Laboratory of Integrative Cancer Immunology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Kent W HunterLaboratory of Cancer Biology and Genetics, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA. Electronic address: hunterk@mail.nih.gov.

Funding

Intramural NIH HHS Z99 CA999999
6 · The paper itself

Abstract

Protein and RNA acetylation are crucial for development and cancer progression. NAT10 is the only known acetyltransferase responsible for N4-acetylcytidine (ac4C) modification of RNA. However, the mechanism by which NAT10 contributes to cancer progression remains unclear. Here, we show that NAT10 interacts with a mechanosensitive, metastasis-susceptibility protein complex at the nuclear pore. Loss of NAT10's acetylation activity significantly reduces lung metastasis in both allograft and genetically engineered mouse models of breast cancer. Unexpectedly, upon NAT10 knockout, loss of ac4C modification in chromatin-associated tRNAs disrupts p300/CBP function, resulting in genome-wide chromatin reorganization and altered expression of genes that recruit metastasis-promoting myeloid cells to the tumor microenvironment. These findings highlight a role for NAT10 in regulating enhancer activity in metastatic tumor cells and reveal its impact on tumor-immune interactions that contribute to metastatic progression.

Indexed as

Breast NeoplasmsChromatinLung NeoplasmsN-Terminal Acetyltransferase Ep300-CBP Transcription FactorsRNA, TransferAcetylationAnimalsCell Line, TumorFemaleGene Expression Regulation, NeoplasticHumansMiceMice, KnockoutNeoplasm MetastasisN-Terminal AcetyltransferasesChromatinNAT10 protein, humanN-Terminal Acetyltransferase EN-Terminal Acetyltransferasesp300-CBP-Associated Factorp300-CBP Transcription FactorsRNA, TransferacetylationchromatinenhancermetastasisneutrophilstranscriptiontRNAtumor microenvironment

Identifiers

PMID41344331
PMCPMC12709618

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.