Evidence map›Paper›PMID 36803422›Full record

ArticleEpigenetics & chromatin2023

Proximity labeling reveals a new in vivo network of interactors for the histone demethylase KDM5.

Matanel Yheskel, Simone Sidoli, Julie Secombe

Open access · goldAbstract read
In one paragraph

Article in Epigenetics & chromatin, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  6. Review
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  9. Review
  10. The Intellectual Disability Risk GeneThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  11. Article
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  13. Review
  14. 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

3 authors at 1 institution in 1 country.

Matanel YheskelDepartment of Genetics, Albert Einstein College of Medicine, Bronx, NY, USA.
Simone SidoliDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.
Julie SecombeDepartment of Genetics, Albert Einstein College of Medicine, Bronx, NY, USA. julie.secombe@einsteinmed.edu.
Albert Einstein College of Medicine · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI Ulrich Steidl · 1985 to 2026
$111.2M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
SUPPORT FOR THE ROSE F KENNEDY IDDRC P50P50HD105352 · NICHD · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SOPHIE MOLHOLM, Steven Upshaw Walkley · 2021 to 2026
$7.0M
Distinct Modes of Gene Regulation by KDM5R01GM112783 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SECOMBE, JULIE · 2015 to 2023
$3.0M
Orbitrap Exploris 480 Basic SystemS10OD030286 · OD · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SIDOLI, SIMONE · 2021 to 2021
$600k
Epigenetic and transcriptional consequences of Intellectual Disability-associated mutations in the histone lysine demethylase KDM5.F31GM146347 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI YHESKEL, MATANEL · 2022 to 2024
$143k
NCI NIH HHS P30 CA013330NICHD NIH HHS P50 HD105352NIGMS NIH HHS F31 GM146347NIGMS NIH HHS R01 GM112783NIGMS NIH HHS T32 GM007288NIH HHS S10 OD030286
6 · The paper itself

Abstract

backgroundKDM5 family proteins are multi-domain regulators of transcription that when dysregulated contribute to cancer and intellectual disability. KDM5 proteins can regulate transcription through their histone demethylase activity in addition to demethylase-independent gene regulatory functions that remain less characterized. To expand our understanding of the mechanisms that contribute to KDM5-mediated transcription regulation, we used TurboID proximity labeling to identify KDM5-interacting proteins.

resultsUsing Drosophila melanogaster, we enriched for biotinylated proteins from KDM5-TurboID-expressing adult heads using a newly generated control for DNA-adjacent background in the form of dCas9:TurboID. Mass spectrometry analyses of biotinylated proteins identified both known and novel candidate KDM5 interactors, including members of the SWI/SNF and NURF chromatin remodeling complexes, the NSL complex, Mediator, and several insulator proteins.

conclusionsCombined, our data shed new light on potential demethylase-independent activities of KDM5. In the context of KDM5 dysregulation, these interactions may play key roles in the alteration of evolutionarily conserved transcriptional programs implicated in human disorders.

Indexed as

Drosophila melanogasterDrosophila ProteinsHistone DemethylasesAnimalsCell NucleusGene Expression RegulationDrosophila ProteinsHistone DemethylasesLid protein, DrosophilaChromatin modifiersHistone demethylaseInsulatorsKDM5Mass spectrometryProximity labelingTurboID

Identifiers

PMID36803422
PMCPMC9938590
OpenAlexW4321275913

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.