PCAF and SIRT1 modulateβTrCP1 protein stability in an acetylation-dependent manner

作     者：Fabin Dang Cong Jiang Tao Zhang Hiroyuki Inuzuka Wenyi Wei Fabin Dang;Cong Jiang;Tao Zhang;Hiroyuki Inuzuka;Wenyi Wei

作者机构：Department of PathologyBeth Israel Deaconess Medical CenterHarvard Medical SchoolBostonMA 02215USA 

出 版 物：《Journal of Genetics and Genomics》 (遗传学报（英文版）)

年 卷 期：2021年第48卷第7期

页      面：652-655页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 071007[理学-遗传学] 

基　　金：supported in part by 1K99CA263194 to F.D. R01CA229307 R35CA253027 to W.W 

主　　题：stability steps catalyzed 

摘      要：Ubiquitination plays critical roles in regulating various physiological events,such as protein degradation,activation,secretion,sorting and trafficking(Dang et al.,2021).The ubiquitination process involves three major steps,catalyzed by ubiquitin-activating enzymes(E1s),ubiquitin-conjugating enzymes(E2s),and ubiquitin ligases(E3s),respectively(Scheffner et al.,1995).