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Protein post-translational modifications in the regulation of cancer hallmarks

Cancer Gene Therapy volume 30, pages 529–547 (2023)Cite this article

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Abstract

Posttranslational modifications (PTMs) of proteins, the major mechanism of protein function regulation, play important roles in regulating a variety of cellular physiological and pathological processes. Although the classical PTMs, such as phosphorylation, acetylation, ubiquitination and methylation, have been well studied, the emergence of many new modifications, such as succinylation, hydroxybutyrylation, and lactylation, introduces a new layer to protein regulation, leaving much more to be explored and wide application prospects. In this review, we will provide a broad overview of the significant roles of PTMs in regulating human cancer hallmarks through selecting a diverse set of examples, and update the current advances in the therapeutic implications of these PTMs in human cancer.

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Fig. 1: Overview of the enzymatic cascade of ubiquitination and ubiquitin-like conjugation.
Fig. 2: Overview of the enzymatic cascade of acylation modification.
Fig. 3: Overview of the enzymatic cascade of methylation.
Fig. 4: PTMs contribute to the “hallmarks of cancer”.

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Acknowledgements

This study was supported by the National Natural Science Foundation of China (81974437, 81472627, 82172959, 81874147). We thank Thomas Luo for editoral assistance.

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  1. Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University Health Science Center, 100191, Beijing, China

    Haiying Wang, Liqian Yang & Jianyuan Luo

  2. Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, 100191, Beijing, China

    Minghui Liu & Jianyuan Luo

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  1. Haiying Wang
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Wang, H., Yang, L., Liu, M. et al. Protein post-translational modifications in the regulation of cancer hallmarks. Cancer Gene Ther 30, 529–547 (2023). https://doi.org/10.1038/s41417-022-00464-3

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