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Updated: May 16, 2025

Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy
Published on: October 18, 2024
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.
Abstract:
Protein post-translational modifications (PTMs) refer to covalent and enzymatic alterations to folded or nascent proteins during or after protein biosynthesis to alter the properties and functions of proteins. PTMs are modified in a variety of types and affect almost all aspects of cell biology. PTMs have been reported to be involved in cancer progression by influencing multiple signaling pathways. The mechanism of action of histone PTMs in cancer has been extensively studied. Notably, evidence is mounting that PTMs of non-histone proteins also play a vital role in cancer progression. In this review, we provide a systematic description of main non-histone PTMs associated with cancer progression, including acetylation, lactylation, methylation, ubiquitination, phosphorylation, and SUMOylation, based on recent studies.
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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