Evidence map›Paper›PMID 34140692›Full record

ArticleNature metabolism2021

Nuclear dihydroxyacetone phosphate signals nutrient sufficiency and cell cycle phase to global histone acetylation.

Jiao-Jiao Zhang, Ting-Ting Fan, Yun-Zi Mao, Jun-Li Hou, Meng Wang, Min Zhang, Yan Lin, Lei Zhang, Guo-Quan Yan, Yan-Peng An and 7 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature metabolism, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

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  11. LncRNA-Mediated TPI1 and PKM2 Promote Self-Renewal and Chemoresistance in GBM.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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  17. Article
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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 1 country.

Jiao-Jiao Zhang *Obstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Ting-Ting Fan *Obstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Yun-Zi Mao *Obstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Jun-Li HouDepartment of Chemistry, Fudan University, Shanghai, China.
Meng WangObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Min ZhangDepartment of Chemistry, Fudan University, Shanghai, China.
Yan LinObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Lei ZhangObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Guo-Quan YanObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Yan-Peng AnObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Jun YaoObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Cheng ZhangObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-9218-5019
Peng-Cheng LinKey Laboratory for Tibet Plateau Phytochemistry of Qinghai Province, College of Pharmacy, Qinghai University for Nationalities, Xining, China.
Yi-Yuan YuanObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.
Jian-Yuan ZhaoObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China.ORCID http://orcid.org/0000-0001-9861-0330
Wei XuObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China. xuwei_0706@fudan.edu.cn.ORCID http://orcid.org/0000-0002-9858-589X
Shi-Min ZhaoObstetrics & Gynecology Hospital of Fudan University, State Key Laboratory of Genetic Engineering, Shanghai Key Laboratory of Metabolic Remodeling, School of Life Sciences and Institutes of Biomedical Sciences, Shanghai, China. zhaosm@fudan.edu.cn.ORCID http://orcid.org/0000-0002-3674-9107
Fudan University · CNQinghai University for Nationalities · CNSichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Global histone acetylation varies with changes in the nutrient and cell cycle phases; however, the mechanisms connecting these variations are not fully understood. Herein, we report that nutrient-related and cell-cycle-regulated nuclear acetate regulates global histone acetylation. Histone deacetylation-generated acetate accumulates in the nucleus and induces histone hyperacetylation. The nuclear acetate levels were controlled by glycolytic enzyme triosephosphate isomerase 1 (TPI1). Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP. CDK2 accumulates in the cytosol during the late G1/S phases. Inactivation or blockade of nuclear translocation of TPI1 abrogates nutrient-dependent and cell-cycle-dependent global histone acetylation, chromatin condensation, gene transcription and DNA replication. These results identify the mechanism of maintaining global histone acetylation by nutrient and cell cycle signals.

Indexed as

Signal TransductionAcetatesAcetylationCell CycleCell Cycle ProteinsCell NucleusChromatinDihydroxyacetone PhosphateDNA ReplicationHistonesHumansNutrientsPhosphorylationTranscription, GeneticAcetatesCell Cycle ProteinsChromatinDihydroxyacetone PhosphateHistonesNutrients

Identifiers

PMID34140692
OpenAlexW3168843438

What OpenQuestion holds

Textmetadata
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.