Evidence map›Paper›PMID 42702606›Full record

ArticleNature communications2026

The RNA helicase domain of NAT10 promotes the biogenesis of hypomodified ribosomes to enhance cancer cell proliferation.

Mahmood H Dalhat, Sharath Narayan, Maria Eleftheriou, James Russell, James Heslop, Hannah Serio, Khulood A Alzahrani, Adam Suh, Ajay Edakkara, Sweta Raikundalia and 14 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

24 authors.

Mahmood H Dalhat *Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Sharath Narayan *Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Maria EleftheriouCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-1842-5838
James RussellCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.
James HeslopCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.
Hannah SerioDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Khulood A AlzahraniDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Adam SuhDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.ORCID http://orcid.org/0009-0007-3422-2313
Ajay EdakkaraCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0009-0000-5159-7175
Sweta RaikundaliaDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Lea LandmannDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Ryan AsbyCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.
Evangelia StamouCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.
Judith LópezCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-3202-9935
Yogeshkumar MalamCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-1192-7560
Demetrios AsprisMRC Toxicology Unit, University of Cambridge, Cambridge, UK.
Emmely A PatrassoDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
Stephanie MouDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-7564-5423
George GiotopoulosCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-1390-6592
Walid T KhaledCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-9068-5776
Brian J P HuntlyCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-0312-161X
Fotios SampaziotisCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-0812-7586
Konstantinos TzelepisCambridge Stem Cell Institute, University of Cambridge, Cambridge, UK. kt404@cam.ac.uk.ORCID http://orcid.org/0000-0002-4865-7648
Daniel ArangoDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA. daniel.arangotamayo@northwestern.edu.ORCID http://orcid.org/0000-0001-9523-830X

Funding

Regulation of translation initiation by the epitranscriptomeR35GM159598 · NIGMS · NORTHWESTERN UNIVERSITY · PI Daniel Arango · 2025 to 2026
$880k
Mechanisms of translation regulation by N4-acetylcytidine in cancer cellsR00CA245035 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ARANGO, DANIEL · 2021 to 2023
$747k
Cancer Research UK (CRUK) SEBCATP-2022/100009Leuka 2022/FuF/001NCI NIH HHS R00 CA245035NIGMS NIH HHS R35 GM159598Wellcome TrustWellcome Trust (Wellcome) 306752/Z/23/Z
6 · The paper itself

Abstract

N-acetyltransferase 10 (NAT10) is a multifunctional enzyme that harbors RNA acetyltransferase and RNA helicase domains and has emerged as a therapeutic vulnerability in solid and hematological malignancies. By coupling Proteolysis Targeting Chimera-mediated degradation of NAT10 with a deep mutational scanning assay, followed by validations in biochemical assays, human cell lines, and female mouse xenografts, we find that the RNA helicase domain of NAT10 enhances cancer cell proliferation and tumor growth. This proliferative function of NAT10 is independent of RNA acetylation but requires its RNA-binding activity. The RNA helicase domain of NAT10 is required for 18S rRNA binding, promoting biogenesis of the 40S ribosomal subunit, while simultaneously interfering with the deposition of the conserved 18S rRNA modification m¹acp³Ψ. Loss of m¹acp³Ψ in 18S rRNA enhances cancer cell proliferation, revealing that NAT10 promotes the biogenesis of hypomodified ribosomes to facilitate tumor growth. These findings uncover a mechanism by which NAT10 promotes cancer cell proliferation and establish its RNA helicase domain as a potential therapeutic target.

Indexed as

AcetyltransferasesCell ProliferationNeoplasmsN-Terminal Acetyltransferase ERibosomesRNA HelicasesAnimalsCell Line, TumorFemaleHumansMiceN-Terminal AcetyltransferasesProtein DomainsRibosome Subunits, Small, EukaryoticRNA, Ribosomal, 18SAcetyltransferasesNAT10 protein, humanN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesRNA HelicasesRNA, Ribosomal, 18S

Identifiers

PMID42702606
PMCPMC13547379

What Socratic holds

Textmetadata
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.