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Updated: Sep 17, 2025

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Reversible Acetylation of Non-histone Proteins in Human Cancers

Chunran Feng1, Yiqun Zeng1, Edward V Prochownik2

  • 1Department of Colorectal and Anal Surgery, Zhongnan Hospital of Wuhan University, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Medical Research Institute, TaiKang Center for Life and Medical Sciences, Wuhan University, Wuhan, China.

Results and Problems in Cell Differentiation
|July 1, 2025
PubMed

Insights

Reversible acetylation of non-histone proteins is crucial in cancer. This review covers histone acetyltransferases (HATs) and deacetylases (HDACs) and their inhibitors for cancer therapy.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Reversible acetylation of non-histone proteins has been extensively studied over the past 30 years.
  • Understanding its mechanisms and functional consequences is key to deciphering cellular processes.

Purpose of the Study:

  • To review histone acetyltransferases (HATs) and deacetylases (HDACs) and their inhibitors.
  • To focus on the role of reversible acetylation in tumor development.
  • To explore the therapeutic applications of HAT and HDAC inhibitors in cancer.

Main Methods:

  • Literature review of HATs and HDACs.
  • Analysis of the role of protein acetylation in tumorigenesis.
  • Evaluation of HAT and HDAC inhibitors in preclinical and clinical cancer studies.

Main Results:

  • Significant progress has been made in understanding protein acetylation.
  • Reversible acetylation plays a critical role in various aspects of tumor development.
  • HAT and HDAC inhibitors show promise as cancer therapeutics.

Conclusions:

  • Reversible acetylation is a vital regulatory mechanism in cancer.
  • Targeting HATs and HDACs offers a promising strategy for cancer treatment.
  • Further research into HAT/HDAC inhibitors is warranted for effective cancer therapy.
Keywords:
Cancer therapyHistone acetyltransferasesHistone deacetylasesReversible acetylation of non-histone protein

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