Evidence map›Paper›PMID 32610040›Full record

ArticleCell stem cell2020

Histone Acetyltransferase MOF Blocks Acquisition of Quiescence in Ground-State ESCs through Activating Fatty Acid Oxidation.

Le Tran Phuc Khoa, Yao-Chang Tsan, Fengbiao Mao, Daniel M Kremer, Peter Sajjakulnukit, Li Zhang, Bo Zhou, Xin Tong, Natarajan V Bhanu, Chunaram Choudhary and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell stem cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.9field-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

39 citing papers in PubMed, 61 citations in OpenAlex.

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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 3 institutions in 2 countries.

Le Tran Phuc KhoaDepartment of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Yao-Chang TsanDepartment of Human Genetics, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Fengbiao MaoDepartment of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Daniel M KremerDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Peter SajjakulnukitDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Li ZhangDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Bo ZhouDepartment of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Xin TongDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Natarajan V BhanuEpigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Chunaram ChoudharyDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen N, Denmark.
Benjamin A GarciaEpigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Lei YinDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Gary D SmithDepartment of Obstetrics and Gynecology, University of Michigan, Ann Arbor, MI 48109, USA.
Thomas L SaundersDepartment of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.
Stephanie L BielasDepartment of Human Genetics, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Costas A LyssiotisDepartment of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Yali DouDepartment of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. Electronic address: yalidou@usc.edu.
University of Michigan–Ann Arbor · USUniversity of Pennsylvania · USNovo Nordisk Foundation · DK

Funding

XenograftP30CA046592 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI THEODORE S LAWRENCE · 1988 to 2026
$178.2M
Statistics and Bioinformatics Core - WangU24DK097153 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BURANT, CHARLES F · 2012 to 2017
$10.1M
Function of MLL in transcription regulationR01GM082856 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DOU, YALI · 2009 to 2023
$4.0M
Enhancer Dysregulation in AMLR01CA232263 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DOU, YALI · 2019 to 2023
$2.7M
Role of histone ubiquitination in neurodevelopment and diseaseR01NS101597 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BIELAS, STEPHANIE LEE · 2018 to 2022
$2.0M
Role and Mechanisms of E4BP4 over-activation in diet-induced fatty liver diseaseR01DK121170 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TONG, XIN · 2019 to 2022
$1.6M
NCI NIH HHS P30 CA046592NCI NIH HHS R01 CA232263NIDDK NIH HHS R01 DK121170NIDDK NIH HHS U24 DK097153NIGMS NIH HHS R01 GM082856NINDS NIH HHS R01 NS101597
6 · The paper itself

Abstract

Self-renewing embryonic stem cells (ESCs) respond to environmental cues by exiting pluripotency or entering a quiescent state. The molecular basis underlying this fate choice remains unclear. Here, we show that histone acetyltransferase MOF plays a critical role in this process through directly activating fatty acid oxidation (FAO) in the ground-state ESCs. We further show that the ground-state ESCs particularly rely on elevated FAO for oxidative phosphorylation (OXPHOS) and energy production. Mof deletion or FAO inhibition induces bona fide quiescent ground-state ESCs with an intact core pluripotency network and transcriptome signatures akin to the diapaused epiblasts in vivo. Mechanistically, MOF/FAO inhibition acts through reducing mitochondrial respiration (i.e., OXPHOS), which in turn triggers reversible pluripotent quiescence specifically in the ground-state ESCs. The inhibition of FAO/OXPHOS also induces quiescence in naive human ESCs. Our study suggests a general function of the MOF/FAO/OXPHOS axis in regulating cell fate determination in stem cells.

Indexed as

Embryonic Stem CellsHistone AcetyltransferasesCell DifferentiationCell DivisionFatty AcidsHumansFatty AcidsHistone Acetyltransferasescell fate decisionembryo developmentepigeneticsFAOMOFquiescenceself-renewalstem cell metabolism

Identifiers

PMID32610040
PMCPMC7758074
OpenAlexW3038881037

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.