Evidence map›Paper›PMID 33372411›Full record

ArticleEMBO reports2021

Histone acetyltransferase 1 is a succinyltransferase for histones and non-histones and promotes tumorigenesis.

Guang Yang, Ying Yuan, Hongfeng Yuan, Jiapei Wang, Haolin Yun, Yu Geng, Man Zhao, Linhan Li, Yejing Weng, Zixian Liu and 5 more

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

110 citing papers in PubMed, 148 citations in OpenAlex.

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  6. Stage-Specific H3K14 and H3K23 Succinylation Orchestrates Insect Metamorphosis and Oogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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50 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Guang YangDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Ying YuanDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Hongfeng YuanDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Jiapei WangDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Haolin YunDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Yu GengDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Man ZhaoDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Linhan LiJingjie PTM BioLab Co. Ltd., Hangzhou Economic and Technological Development Area, Hangzhou, China.
Yejing WengJingjie PTM BioLab Co. Ltd., Hangzhou Economic and Technological Development Area, Hangzhou, China.
Zixian LiuDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Jinyan FengDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Yanan BuDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Lei LiuDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.
Bingnan WangJingjie PTM BioLab Co. Ltd., Hangzhou Economic and Technological Development Area, Hangzhou, China.
Xiaodong ZhangDepartment of Cancer Research, Institute of Molecular Biology, College of Life Sciences, Nankai University, Tianjin, China.ORCID 0000-0002-6891-9019
Nankai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine succinylation (Ksucc) is an evolutionarily conserved and widespread post-translational modification. Histone acetyltransferase 1 (HAT1) is a type B histone acetyltransferase, regulating the acetylation of both histone and non-histone proteins. However, the role of HAT1 in succinylation modulation remains unclear. Here, we employ a quantitative proteomics approach to study succinylation in HepG2 cancer cells and find that HAT1 modulates lysine succinylation on various proteins including histones and non-histones. HAT1 succinylates histone H3 on K122, contributing to epigenetic regulation and gene expression in cancer cells. Moreover, HAT1 catalyzes the succinylation of PGAM1 on K99, resulting in its increased enzymatic activity and the stimulation of glycolytic flux in cancer cells. Clinically, HAT1 is significantly elevated in liver cancer, pancreatic cancer, and cholangiocarcinoma tissues. Functionally, HAT1 succinyltransferase activity and the succinylation of PGAM1 by HAT1 play critical roles in promoting tumor progression in vitro and in vivo. Thus, we conclude that HAT1 is a succinyltransferase for histones and non-histones in tumorigenesis.

Indexed as

Epigenesis, GeneticHistonesAcetylationCarcinogenesisHep G2 CellsHistone AcetyltransferasesHumansHistone Acetyltransferaseshistone acetyltransferase type B complexHistonesepigenetic regulationglycolysisHAT1succinylationtumorigenesis

Identifiers

PMID33372411
PMCPMC7857430
OpenAlexW3117217775

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.