Control of protein stability by post-translational modifications

被引:253
|
作者
Lee, Ji Min [1 ]
Hammaren, Henrik M. [2 ]
Savitski, Mikhail M. [2 ]
Baek, Sung Hee [3 ]
机构
[1] Korea Adv Inst Sci & Technol, Grad Sch Med Sci & Engn, Daejeon 34141, South Korea
[2] European Mol Biol Lab, Genome Biol Unit, D-69117 Heidelberg, Germany
[3] Seoul Natl Univ, Creat Res Initiat Ctr Epigenet Code & Dis, Sch Biol Sci, Seoul 08826, South Korea
基金
新加坡国家研究基金会;
关键词
PHOSPHORYLATION-DEPENDENT UBIQUITINATION; ESTROGEN-RECEPTOR-ALPHA; F-BOX PROTEIN; C-MYC; LYSINE METHYLATION; BETA-CATENIN; P53; ACETYLATION; CELL-CYCLE; FUNCTIONAL INTERACTION; ARGININE METHYLATION;
D O I
10.1038/s41467-023-35795-8
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Post-translational modifications (PTMs) can occur on specific amino acids localized within regulatory domains of target proteins, which control a protein's stability. These regions, called degrons, are often controlled by PTMs, which act as signals to expedite protein degradation (PTM-activated degrons) or to forestall degradation and stabilize a protein (PTM-inactivated degrons). We summarize current knowledge of the regulation of protein stability by various PTMs. We aim to display the variety and breadth of known mechanisms of regulation as well as highlight common themes in PTM-regulated degrons to enhance potential for identifying novel drug targets where druggable targets are currently lacking. Here the authors summarize current knowledge of the regulation of protein stability by various post-translational modifications (PTMs) including methylation and phosphorylation. PTM-regulated degrons act as signals for protein degradation or stabilization.
引用
收藏
页数:16
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