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Research progress in protein post-translational modification

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Chinese Science Bulletin

Abstract

Protein post-translational modification plays an important role in organism. It makes the protein obtain more complicated structures, perfect functions, more accurate regulations and more specific operations. The most common protein post-translational modifications include ubiquitylation, phosphorylation, glycosylation, lipodation, methylation, and acetylation and so on. Ubiquitylation plays an essential role in cellular functions such as cellular differentiation, apoptosis, DNA repair, antigen processing, and stress response. Phosphorylation is related to physiological and pathological processes including cellular signal conduction, nervous activity, muscle contraction and proliferation, development and differentiation of cells. Protein glycosylation is of great importance for many cell processes like immunoprotection, virus replication, cell growth, and occurrence of inflammation and so on. Lipodation is vital to signal conduction. Histone methylation and acetylation are responsible for transcription regulation. In vivo, different post-translational modifications do not occur isolatedly, but influence each other’s function and cooperate with each other. Understanding what influences the post-translational modifications will help to uncover cellular processes and protein network in molecular level and finally direct more precise drug design targeting molecules. Post-translational modification mimics are set to dominate the next wave of protein therapeutics and become powerful medicinal tools in the 21st century.

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Authors and Affiliations

  1. Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Department of Chemistry, Tsinghua University, Beijing, 100084, China

    Hu Jia, Guo Yanting & Li Yanmei

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  1. Hu Jia
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  2. Guo Yanting
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  3. Li Yanmei
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Correspondence to Li Yanmei.

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Hu, J., Guo, Y. & Li, Y. Research progress in protein post-translational modification. CHINESE SCI BULL 51, 633–645 (2006). https://doi.org/10.1007/s11434-006-0633-3

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  • DOI: https://doi.org/10.1007/s11434-006-0633-3

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