N-myristoylation: from cell biology to translational medicine

被引:59
作者
Yuan, Meng [1 ]
Song, Zi-han [1 ]
Ying, Mei-dan [1 ]
Zhu, Hong [1 ]
He, Qiao-jun [1 ]
Yang, Bo [1 ]
Cao, Ji [1 ]
机构
[1] Zhejiang Univ, Coll Pharmaceut Sci, Zhejiang Prov Key Lab Anticanc Drug Res, Hangzhou 310058, Peoples R China
基金
中国国家自然科学基金;
关键词
N-myristoylation; N-myristoyltransferase; infectious diseases; parasitic diseases; cancers; translational medicine; MEMBRANE-BINDING; TERMINAL REGION; PLASMA-MEMBRANE; 26S PROTEASOME; PROTEIN; MYRISTOYLTRANSFERASE; SRC; DOMAIN; SWITCH; ACTIVATION;
D O I
10.1038/s41401-020-0388-4
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:1005 / 1015
页数:11
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