Evidence map›Paper›PMID 37398291›Full record

ArticlebioRxiv : the preprint server for biology2024

KDM3A and KDM3B Maintain Naïve Pluripotency Through the Regulation of Alternative Splicing.

Caleb M Dillingham, Harshini Cormaty, Ellen C Morgan, Andrew I Tak, Dakarai E Esgdaille, Paul L Boutz, Rupa Sridharan

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 1 citations in OpenAlex.

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

7 authors at 2 institutions in 1 country.

Caleb M DillinghamWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI, 53715, USA.
Harshini CormatyWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI, 53715, USA.
Ellen C MorganWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI, 53715, USA.
Andrew I TakWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI, 53715, USA.
Dakarai E EsgdailleDepartment of Biochemistry and Biophysics, Center for RNA Biology, Wilmot Cancer Center, University of Rochester School of Medicine and Dentistry.
Paul L BoutzDepartment of Biomedical Genetics, University of Rochester School of Medicine and Dentistry.
Rupa SridharanWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI, 53715, USA.
University of Wisconsin–Madison · USUniversity of Rochester · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007133 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PERNA, NICOLE T · 1985 to 2023
$16.5M
Training in Wellness and Resiliency at the University of Rochester Medical Center and College of Arts, Sciences & EngineeringT32GM135134 · NIGMS · UNIVERSITY OF ROCHESTER · PI Jeffrey J Hayes, Lynne E Maquat · 2020 to 2026
$2.9M
Histone Demethylase Control of Post Implantation DevelopmentR01HD105151 · NICHD · UNIVERSITY OF WISCONSIN-MADISON · PI Rupa Sridharan · 2022 to 2026
$1.9M
Genomics-based approaches to understanding mechanistic alterations of spliceosome function in disease statesR01GM141544 · NIGMS · UNIVERSITY OF ROCHESTER · PI BOUTZ, PAUL LAWRENCE · 2021 to 2025
$1.6M
Histone demethylase control of primordial germ cell specificationF31HD113347 · NICHD · UNIVERSITY OF WISCONSIN-MADISON · PI Harshini Cormaty · 2024 to 2026
$125k
NICHD NIH HHS F31 HD113347NICHD NIH HHS R01 HD105151NIGMS NIH HHS R01 GM141544NIGMS NIH HHS T32 GM007133NIGMS NIH HHS T32 GM135134
6 · The paper itself

Abstract

Histone modifying enzymes play a central role in maintaining cell identity by establishing a conducive chromatin environment for lineage specific transcription factor activity. Pluripotent embryonic stem cell (ESC) identity is characterized by a lower abundance of gene repression associated histone modifications that enables rapid response to differentiation cues. The KDM3 family of histone demethylases removes the repressive histone H3 lysine 9 dimethylation (H3K9me2). Here we uncover a surprising role for the KDM3 proteins in the maintenance of the pluripotent state through post-transcriptional regulation. We find that KDM3A and KDM3B interact with RNA processing factors such as EFTUD2 and PRMT5. Acute selective degradation of the endogenous KDM3A and KDM3B proteins resulted in altered splicing independent of H3K9me2 status or catalytic activity. These splicing changes partially resemble the splicing pattern of the more blastocyst-like ground state of pluripotency and occurred in important chromatin and transcription factors such as

Identifiers

PMID37398291
PMCPMC10312572
OpenAlexW4378977613

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.