Abstract
Various lipids and lipid metabolites are bound to and modify the proteins in eukaryotic cells, which are known as ‘protein lipidation’. There are four major types of the protein lipidation, i.e. myristoylation, palmitoylation, prenylation, and glycosylphosphatidylinositol anchor. N-myristoylation refers to the attachment of 14-carbon fatty acid myristates to the N-terminal glycine of proteins by N-myristoyltransferases (NMT) and affects their physiology such as plasma targeting, subcellular tracking and localization, thereby influencing the function of proteins. With more novel pathogenic N-myristoylated proteins are identified, the N-myristoylation will attract great attentions in various human diseases including infectious diseases, parasitic diseases, and cancers. In this review, we summarize the current understanding of N-myristoylation in physiological processes and discuss the hitherto implication of crosstalk between N-myristoylation and other protein modification. Furthermore, we mention several well-studied NMT inhibitors mainly in infectious diseases and cancers and generalize the relation of NMT and cancer progression by browsing the clinic database. This review also aims to highlight the further investigation into the dynamic crosstalk of N-myristoylation in physiological processes as well as the potential application of protein N-myristoylation in translational medicine.
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Acknowledgements
This work was supported by grants from the National Natural Science Foundation of China (81872885 to J.C.), Zhejiang Provincial Natural Science Foundation (Y18H310005 to J.C.), and the Talent Project of Zhejiang Association for Science and Technology (No. 2018YCGC002 to J.C.).
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MY and JC conceived and designed the review article. MY, ZHS, and JC collected the related research articles contributed to the paper. MY, MDY, HZ, BY, QJH, and JC made amendments to the paper.
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Yuan, M., Song, Zh., Ying, Md. et al. N-myristoylation: from cell biology to translational medicine. Acta Pharmacol Sin 41, 1005–1015 (2020). https://doi.org/10.1038/s41401-020-0388-4
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DOI: https://doi.org/10.1038/s41401-020-0388-4
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