Functions and mechanisms of non-histone post-translational modifications in cancer progression

Zongyang Li1,2, Tao Zhu1, Yushu Wu2

  • 1Department of Urology, The First Affiliated Hospital of Shandong Second Medical University, Weifang, 261041, China.

Cell Death Discovery
|March 31, 2025
PubMed

Insights

Post-translational modifications (PTMs) of non-histone proteins, including acetylation and phosphorylation, are increasingly recognized for their crucial roles in cancer progression. This review details key PTMs impacting cancer signaling pathways.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Protein post-translational modifications (PTMs) are vital enzymatic alterations affecting protein function and cell biology.
  • While histone PTMs in cancer are well-studied, non-histone protein PTMs are emerging as critical regulators of cancer progression.
  • PTMs influence numerous signaling pathways implicated in various cancers.

Purpose of the Study:

  • To systematically review the role of major non-histone protein PTMs in cancer progression.
  • To highlight recent findings on PTMs like acetylation, lactylation, methylation, ubiquitination, phosphorylation, and SUMOylation in cancer.

Main Methods:

  • Literature review of recent studies on non-histone protein PTMs and cancer.
  • Systematic description of PTM types and their involvement in cancer signaling.

Main Results:

  • Non-histone protein PTMs significantly impact multiple signaling pathways driving cancer progression.
  • Specific PTMs discussed include acetylation, lactylation, methylation, ubiquitination, phosphorylation, and SUMOylation.
  • Evidence supports a vital role for these modifications in cancer development and advancement.

Conclusions:

  • Non-histone protein PTMs are critical players in cancer biology.
  • Targeting these PTMs may offer novel therapeutic strategies for cancer treatment.
  • Further research into the mechanisms of non-histone PTMs in cancer is warranted.

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