Evidence map›Paper›PMID 39088653›Full record

ArticleScience (New York, N.Y.)2024

Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex.

Zhenlin Yang, Amel Mameri, Claudia Cattoglio, Catherine Lachance, Alfredo Jose Florez Ariza, Jie Luo, Jonathan Humbert, Deepthi Sudarshan, Arul Banerjea, Maxime Galloy and 5 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Mechanistic insights into INO80-type chromatin remodelers.Current opinion in structural biology · 2025
    Review
  16. Review
  17. Article
  18. Cryo-EM structures reveal the acetylation process of piccolo NuA4.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. BRD8 Guards the Pluripotent State by Sensing and Maintaining Histone Acetylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  20. 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

15 authors.

Zhenlin Yang *California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0002-0076-5068
Amel Mameri *St-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0001-7501-2952
Claudia CattoglioHoward Hughes Medical Institute, University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0001-6100-0491
Catherine LachanceSt-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0009-0007-4675-6398
Alfredo Jose Florez ArizaCalifornia Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0003-2429-4659
Jie LuoInstitute for Systems Biology, Seattle, WA, USA.ORCID 0000-0003-2815-2682
Jonathan HumbertSt-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0002-1090-6207
Deepthi SudarshanSt-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0002-8318-8314
Arul BanerjeaDepartment of Molecular and Cell Biology, University of California, Berkeley, CA, USA.ORCID 0000-0002-0063-0649
Maxime GalloySt-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0002-8747-0819
Amélie Fradet-TurcotteSt-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0002-5431-8650
Jean-Philippe LambertEndocrinology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0002-0833-1221
Jeff A RanishInstitute for Systems Biology, Seattle, WA, USA.ORCID 0000-0001-7181-0287
Jacques CôtéSt-Patrick Research Group in Basic Oncology, Oncology Division of the CHU de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, QC, Canada.ORCID 0000-0001-6751-555X
Eva NogalesCalifornia Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, CA, USA.ORCID 0000-0001-9816-3681

Funding

Structural studies of function and regulation of microtubules and transcriptional gene expression machineryR35GM127018 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Eva Nogales · 2018 to 2026
$4.3M
The Expedit-Isotopomeric CrossLinking Mass Spectrometry (Expedit-ICLMS) technology for mapping global and dynamic protein-protein interaction networksR01GM136974 · NIGMS · INSTITUTE FOR SYSTEMS BIOLOGY · PI RANISH, JEFFREY A · 2020 to 2023
$2.0M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM136974NIGMS NIH HHS R35 GM127018
6 · The paper itself

Abstract

The human nucleosome acetyltransferase of histone H4 (NuA4)/Tat-interactive protein, 60 kilodalton (TIP60) coactivator complex, a fusion of the yeast switch/sucrose nonfermentable related 1 (SWR1) and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4, H2A, and H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the E1A binding protein P400 (EP400) subunit serves as a scaffold holding the different functional modules in specific positions, creating a distinct arrangement of the actin-related protein (ARP) module. EP400 interacts with the transformation/transcription domain-associated protein (TRRAP) subunit by using a footprint that overlaps with that of the Spt-Ada-Gcn5 acetyltransferase (SAGA) complex, preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome, emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly.

Indexed as

Chromatin Assembly and DisassemblyLysine Acetyltransferase 5AcetylationAdaptor Proteins, Signal TransducingCryoelectron MicroscopyDNA-Binding ProteinsHistonesHumansNuclear ProteinsNucleosomesProtein DomainsTranscription FactorsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsHistonesKAT5 protein, humanLysine Acetyltransferase 5Nuclear ProteinsNucleosomesTranscription Factorstransformation-transcription domain-associated protein

Identifiers

PMID39088653
PMCPMC11995519

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.