Site-specific chemical fatty-acylation for gain-of-function analysis of protein S-palmitoylation in live cells

被引：26
|
作者：
Li, Yumeng [1 ]
Wang, Shushu [1 ]
Chen, Yanchi [1 ]
Li, Manjia [1 ]
Dong, Xiaoshu [1 ]
Hang, Howard C. [2 ,3 ,4 ]
Peng, Tao [1 ]
机构：
[1] Peking Univ, Sch Chem Biol & Biotechnol, State Key Lab Chem Oncogen, Shenzhen Grad Sch, Shenzhen 518055, Peoples R China
[2] Rockefeller Univ, Lab Chem Biol & Microbial Pathogenesis, New York, NY 10065 USA
[3] Scripps Res, Dept Immunol & Microbiol, La Jolla, CA 92037 USA
[4] Scripps Res, Dept Chem, La Jolla, CA 92037 USA
来源：
CHEMICAL COMMUNICATIONS | 2020年 / 56卷 / 89期
基金：
中国国家自然科学基金;
关键词：
DIELS-ALDER REACTIONS; MAMMALIAN-CELLS; RAS; LIGATION;
D O I：
10.1039/d0cc06073a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Protein S-palmitoylation, or S-fatty-acylation, regulates many fundamental cellular processes in eukaryotes. Herein, we present a chemical fatty-acylation approach that involves site-specific incorporation of cycloalkyne-containing unnatural amino acids and subsequent bioorthogonal reactions with fatty-acyl tetrazines to install fatty-acylation mimics at target protein sites, allowing gain-of-function analysis of S-palmitoylation in live cells.
引用
收藏
页码：13880 / 13883
页数：4
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