Evidence map›Paper›PMID 38448574›Full record

ArticleNature structural & molecular biology2024

Guiding the HBO1 complex function through the JADE subunit.

Nitika Gaurav, Akinori Kanai, Catherine Lachance, Khan L Cox, Jiuyang Liu, Adrian T Grzybowski, Nehmé Saksouk, Brianna J Klein, Yosuke Komata, Shuhei Asada and 5 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 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
3.0field-weighted citation impact, top 8% 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, 13 citations in OpenAlex.

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  15. HBO1, a MYSTerious KAT and its links to cancer.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    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

15 authors at 9 institutions in 3 countries.

Nitika Gaurav *Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO, USA.
Akinori Kanai *Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Japan.ORCID http://orcid.org/0000-0003-1555-6768
Catherine Lachance *Laval University Cancer Research Center, CHU de Québec-UL Research Center-Oncology Division, Quebec City, Québec, Canada.
Khan L CoxDepartment of Physics, Ohio State University, Columbus, OH, USA.
Jiuyang LiuDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO, USA.
Adrian T GrzybowskiDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-7340-9603
Nehmé SaksoukLaval University Cancer Research Center, CHU de Québec-UL Research Center-Oncology Division, Quebec City, Québec, Canada.
Brianna J KleinDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO, USA.
Yosuke KomataTsuruoka Metabolomics Laboratory, National Cancer Center, Tsuruoka, Japan.
Shuhei AsadaDepartment of Radiation Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0001-6116-7996
Alexander J RuthenburgDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0003-2709-4564
Michael G PoirierDepartment of Physics, Ohio State University, Columbus, OH, USA.
Jacques CôtéLaval University Cancer Research Center, CHU de Québec-UL Research Center-Oncology Division, Quebec City, Québec, Canada. jacques.cote@crchudequebec.ulaval.ca.ORCID http://orcid.org/0000-0001-6751-555X
Akihiko YokoyamaTsuruoka Metabolomics Laboratory, National Cancer Center, Tsuruoka, Japan. ayokoyam@ncc-tmc.jp.ORCID http://orcid.org/0000-0002-5639-8068
Tatiana G KutateladzeDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO, USA. tatiana.kutateladze@cuanschutz.edu.ORCID http://orcid.org/0000-0001-7375-6990
University of Colorado Denver · USNational Institute of Technology, Tsuruoka College · JPThe Ohio State University · USUniversité Laval · CAUniversity of Chicago · USHarvard University · USHôtel-Dieu de Québec · CAThe University of Tokyo · JPUniversity of Colorado Anschutz Medical Campus · US

Funding

Mechanisms of chromatin regulation of transcriptionR35GM139564 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2021 to 2025
$3.6M
Targeting acetylated histone H4 by MLL4R01AG067664 · NIA · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2021 to 2025
$2.1M
Defining the mechanisms of epigenetic information flowR35GM145373 · NIGMS · UNIVERSITY OF CHICAGO · PI Alexander Jackson Ruthenburg · 2022 to 2026
$2.1M
Molecular analysis of ASH1LR01CA252707 · NCI · UNIVERSITY OF COLORADO DENVER · PI TATIANA G KUTATELADZE · 2020 to 2026
$1.9M
The role of JADE in HBO complexesR01HL151334 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2020 to 2023
$1.8M
Quantitatively probing intra-nucleosomal chromatin variation and functionR01GM115945 · NIGMS · UNIVERSITY OF CHICAGO · PI RUTHENBURG, ALEXANDER JACKSON · 2016 to 2020
$1.6M
Epigenetic mechanisms for regulation of p300R01GM135671 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2020 to 2023
$1.4M
Understanding how two related mammalian histone acetyl transferase co-activators, SAGA and ATAC, differentially regulate chromatin dynamics and transcriptionR01GM131626 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2019 to 2021
$1.3M
Interdomain crosstalk in MORC3R01GM125195 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2017 to 2021
$1.3M
Targeting acetylated histone H4 by MLL4R56AG067664 · NIA · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2020 to 2020
$512k
NCI NIH HHS R01 CA252707NHLBI NIH HHS R01 HL151334NIA NIH HHS R01 AG067664NIA NIH HHS R56 AG067664NIGMS NIH HHS R01 GM115945NIGMS NIH HHS R01 GM125195NIGMS NIH HHS R01 GM131626NIGMS NIH HHS R01 GM135671NIGMS NIH HHS R35 GM139564NIGMS NIH HHS R35 GM145373
6 · The paper itself

Abstract

JADE is a core subunit of the HBO1 acetyltransferase complex that regulates developmental and epigenetic programs and promotes gene transcription. Here we describe the mechanism by which JADE facilitates recruitment of the HBO1 complex to chromatin and mediates its enzymatic activity. Structural, genomic and complex assembly in vivo studies show that the PZP (PHD1-zinc-knuckle-PHD2) domain of JADE engages the nucleosome through binding to histone H3 and DNA and is necessary for the association with chromatin targets. Recognition of unmethylated H3K4 by PZP directs enzymatic activity of the complex toward histone H4 acetylation, whereas H3K4 hypermethylation alters histone substrate selectivity. We demonstrate that PZP contributes to leukemogenesis, augmenting transforming activity of the NUP98-JADE2 fusion. Our findings highlight biological consequences and the impact of the intact JADE subunit on genomic recruitment, enzymatic function and pathological activity of the HBO1 complex.

Indexed as

Histone AcetyltransferasesHistonesAcetylationAnimalsChromatinHomeodomain ProteinsHumansMethylationMiceModels, MolecularNucleosomesProtein BindingProtein DomainsTumor Suppressor ProteinsChromatinHistone AcetyltransferasesHistonesHomeodomain ProteinsJADE1 protein, humanKAT7 protein, humanNucleosomesTumor Suppressor Proteins

Identifiers

PMID38448574
PMCPMC11320721
OpenAlexW4392508897

What OpenQuestion holds

Textmetadata
LicenceTDM
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.