Evidence map›Paper›PMID 40347473›Full record

ArticleCell reports2025

PNUTS:PP1 recruitment to Tox4 regulates chromosomal dispersal in Drosophila germline development.

Louise Duncalf, Xinru Wang, Abdulrahman A Aljabri, Amy E Campbell, Rawan Q Alharbi, Ian Donaldson, Andrew Hayes, Wolfgang Peti, Rebecca Page, Daimark Bennett

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PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Louise DuncalfFaculty of Health and Life Sciences, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB Liverpool, UK.
Xinru WangDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA.
Abdulrahman A AljabriFaculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, M13 9PT Manchester, UK; Department of Pharmacology and Toxicology, College of Pharmacy, Taibah University, Madinah, Kingdom of Saudi Arabia.
Amy E CampbellFaculty of Health and Life Sciences, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB Liverpool, UK.
Rawan Q AlharbiFaculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, M13 9PT Manchester, UK.
Ian DonaldsonFaculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, M13 9PT Manchester, UK.
Andrew HayesFaculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, M13 9PT Manchester, UK.
Wolfgang PetiDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, USA.
Rebecca PageDepartment of Cell Biology, University of Connecticut Health Center, Farmington, CT, USA. Electronic address: rpage@uchc.edu.
Daimark BennettFaculty of Health and Life Sciences, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB Liverpool, UK; Faculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, M13 9PT Manchester, UK. Electronic address: daimark.bennett@manchester.ac.uk.

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
Protein Phosphatase 1 Holoenzyme FormationR01GM144483 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI PETI, WOLFGANG · 2022 to 2025
$1.7M
The regulation of phosphoprotein phosphatases in the nucleusR01GM144379 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI Rebecca Page · 2023 to 2026
$1.5M
NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R01 GM144379NIGMS NIH HHS R01 GM144483
6 · The paper itself

Abstract

Ser/Thr protein phosphatase 1 (PP1) forms a large nuclear holoenzyme (with PNUTS, WDR82, and Tox4) whose emerging role is to regulate transcription. However, the role of Tox4, and its interplay with the other phosphatase subunits in this complex, is poorly understood. Here, we combine biochemical, structural, cellular, and in vivo experiments to show that, while tox4 is dispensable for viability, it is essential for fertility, having both PNUTS-dependent and -independent roles in Drosophila germline development. We also show that Tox4 requires zinc for PNUTS TFIIS N-terminal domain (TND) binding, and that it binds the TND on a surface distinct from that used by established TND-interacting transcriptional regulators. We also show that selective disruption of the PNUTS-Tox4 and the PNUTS-PP1 interaction is critical for normal gene expression and chromosomal dispersal during oogenesis. Together, these data demonstrate how interactions within the PNUTS-Tox4-PP1 phosphatase combine to tune transcriptional outputs driving developmental transitions.

Indexed as

Chromosomes, InsectDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsGerm CellsProtein Phosphatase 1AnimalsFemaleGene Expression Regulation, DevelopmentalOogenesisProtein BindingDNA-Binding ProteinsDrosophila ProteinsProtein Phosphatase 1CP: Developmental biologyCP: Molecular biologyDrosophilagermline developmentPNUTSPPP1R10protein phosphatase 1PTW/PP1 complexTox4transcription

Identifiers

PMID40347473
PMCPMC12278311

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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.