Evidence map›Paper›PMID 37294531›Full record

ArticleMolecular biotechnology2024

KAT2A Promotes the Succinylation of PKM2 to Inhibit its Activity and Accelerate Glycolysis of Gastric Cancer.

Chengpeng Zhang, Zonghai Huang

Abstract read
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In one paragraph

Article in Molecular biotechnology, 2024. 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
8.6field-weighted citation impact, top 2% 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, 36 citations in OpenAlex.

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  19. Implication of protein post translational modifications in gastric cancer.Frontiers in cell and developmental biology · 2025
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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

2 authors at 2 institutions in 1 country.

Chengpeng ZhangDepartment of General Surgery, Zhujiang Hospital, Southern Medical University, Guangzhou, 510282, Guangdong, China.
Zonghai HuangDepartment of General Surgery, Zhujiang Hospital, Southern Medical University, Guangzhou, 510282, Guangdong, China. huangzonghai@hotmail.com.ORCID http://orcid.org/0000-0001-8885-3355
First Affiliated Hospital of Guangzhou Medical University · CNZhujiang Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gastric cancer (GC) is one of the main causes of cancer-related death. Lysine acetyltransferases 2 A (KAT2A) is a succinyltransferase that plays an essential role in cancer development. The pyruvate kinase M2 (PKM2) is a glycolysis rate-limiting enzyme that mediates the glycolysis of cancers. This study aimed to explore the effects and mechanism of KAT2A in GC progression. The effects of biological behaviors of GC cells were evaluated by MTT, colony formation and seahorse assays. The succinylation modification was assessed by immunoprecipitation (IP). The interaction between proteins were detected by Co-IP and immunofluorescence. A pyruvate kinase activity detection kit was used to evaluate the activity of PKM2. Western blot was performed to detect the expression and oligomerization of protein. Herein, we confirmed that KAT2A was highly expressed in GC tissues and was associated with a poor prognosis. Function studies showed that knockdown of KAT2A inhibited cell proliferation and glycolytic metabolism of GC. Mechanistically, KAT2A could directly interacted with PKM2 and KAT2A silencing inhibited the succinylation of PKM2 at K475 site. In addition, the succinylation of PKM2 altered its activity rather than its protein levels. Rescue experiments showed that KAT2A promoted GC cell growth, glycolysis, and tumor growth by promoting PKM2 K475 succinylation. Taken together, KAT2A promotes the succinylation of PKM2 at K475 to inhibit PKM2 activity, thus promotes the progression of GC. Therefore, targeting KATA2 and PKM2 may provide novel strategies for the treatment of GC.

Indexed as

Carrier ProteinsCell ProliferationGlycolysisMembrane ProteinsStomach NeoplasmsThyroid Hormone-Binding ProteinsThyroid HormonesAnimalsCell Line, TumorFemaleGene Expression Regulation, NeoplasticHistone AcetyltransferasesHumansMaleMiceMice, Inbred BALB CCarrier ProteinsHistone AcetyltransferasesKAT2A protein, humanMembrane Proteinsp300-CBP-Associated FactorSuccinic AcidThyroid Hormone-Binding ProteinsThyroid HormonesGastric cancerGlycolysisKAT2APKM2Succinylation

Identifiers

PMID37294531
OpenAlexW4379967750

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.