Evidence map›Paper›PMID 38366138›Full record

ArticleNeuropsychopharmacology : official publication of the American College of Neuropsychopharmacology2024

Role of the histone variant H2A.Z.1 in memory, transcription, and alternative splicing is mediated by lysine modification.

Anas Reda, Luca A Hategan, Timothy A B McLean, Samantha D Creighton, Jian Qi Luo, Sean En Si Chen, Shan Hua, Stephen Winston, Isaiah Reeves, Aditya Padmanabhan and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
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

15 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Splice isoforms of the histone variant macroH2A1 differentially regulate hippocampal gene expression and memory formation.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026
    Article
  8. Article
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  10. Article
  11. Review
  12. Review
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  15. 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

17 authors at 5 institutions in 2 countries.

Anas Reda *Department of Cell & Systems Biology, University of Toronto, Toronto, ON, M5S 3G3, Canada.
Luca A Hategan *Department of Cell & Systems Biology, University of Toronto, Toronto, ON, M5S 3G3, Canada.
Timothy A B McLeanDepartment of Cell & Systems Biology, University of Toronto, Toronto, ON, M5S 3G3, Canada.
Samantha D CreightonDepartment of Psychology, University of Toronto Mississauga, Mississauga, ON, L5L 1C6, Canada.
Jian Qi LuoDepartment of Cell & Systems Biology, University of Toronto, Toronto, ON, M5S 3G3, Canada.
Sean En Si ChenDepartment of Cell & Systems Biology, University of Toronto, Toronto, ON, M5S 3G3, Canada.
Shan HuaDepartments of Biology and Biomedical Genetics, University of Rochester Medical Center, Rochester, NY, 14642, USA.
Stephen WinstonDepartment of Surgery and Graduate school of Biomedical Sciences, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
Isaiah ReevesDepartment of Surgery and Graduate school of Biomedical Sciences, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
Aditya PadmanabhanDepartment of Psychology, University of Toronto Mississauga, Mississauga, ON, L5L 1C6, Canada.
Tarkan A DahiDepartment of Biology, University of Toronto Mississauga, Mississauga, ON, L5L 1C6, Canada.
Firyal RamzanDepartment of Biology, University of Waterloo, Waterloo, ON, N2L 3G1, Canada.
Mark A BrimbleDepartment of Host-Microbe Interactions, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
Patrick J MurphyDepartments of Biology and Biomedical Genetics, University of Rochester Medical Center, Rochester, NY, 14642, USA.
Brandon J WaltersDepartment of Biology, University of Toronto Mississauga, Mississauga, ON, L5L 1C6, Canada.
Gilda StefanelliDepartment of Biology, University of Ottawa, Ottawa, ON, K1N 6N5, Canada. gilda.stefanelli@uottawa.ca.
Iva B ZovkicDepartment of Psychology, University of Toronto Mississauga, Mississauga, ON, L5L 1C6, Canada. iva.zovkic@utoronto.ca.ORCID http://orcid.org/0000-0002-4497-6334
University of Toronto · CASt. Jude Children's Research Hospital · USUniversity of Rochester Medical Center · USUniversity of Ottawa · CAUniversity of Waterloo · CA

Funding

Function of Chromatin Features in Cellular ProgrammingR35GM137833 · NIGMS · UNIVERSITY OF ROCHESTER · PI Patrick J. Murphy · 2020 to 2026
$2.8M
Canadian Network for Research and Innovation in Machining Technology, Natural Sciences and Engineering Research Council of Canada (NSERC Canadian Network for Research and Innovation in Machining Technology) RGPIN2020-06911Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada) PJT-156414Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (Conseil de Recherches en Sciences Naturelles et en Génie du Canada) RGPIN-2015-05115NIGMS NIH HHS R35 GM137833
6 · The paper itself

Abstract

Creating long-lasting memories requires learning-induced changes in gene expression, which are impacted by epigenetic modifications of DNA and associated histone proteins. Post-translational modifications (PTMs) of histones are key regulators of transcription, with different PTMs producing unique effects on gene activity and behavior. Although recent studies implicate histone variants as novel regulators of memory, effects of PTMs on the function of histone variants are rarely considered. We previously showed that the histone variant H2A.Z suppresses memory, but it is unclear if this role is impacted by H2A.Z acetylation, a PTM that is typically associated with positive effects on transcription and memory. To answer this question, we used a mutation approach to manipulate acetylation on H2A.Z without impacting acetylation of other histone types. Specifically, we used adeno-associated virus (AAV) constructs to overexpress mutated H2A.Z.1 isoforms that either mimic acetylation (acetyl-mimic) by replacing lysines 4, 7 and 11 with glutamine (KQ), or H2A.Z.1 with impaired acetylation (acetyl-defective) by replacing the same lysines with alanine (KA). Expressing the H2A.Z.1 acetyl-mimic (H2A.Z.1

Indexed as

Alternative SplicingHistonesLysineMemoryProtein Processing, Post-TranslationalTranscription, GeneticAcetylationAnimalsFemaleMaleMiceMice, Inbred C57BLProtein IsoformsH2az1 protein, mouseHistonesLysineProtein Isoforms

Identifiers

PMID38366138
PMCPMC11224360
OpenAlexW4391882901

What OpenQuestion holds

Textmetadata
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.