PUB22 and PUB23 U-box E3 ubiquitin ligases negatively regulate 26S proteasome activity under proteotoxic stress conditions

作     者：Min Yong Ahn Dong Hye Seo Woo Taek Kim Min Yong Ahn;Dong Hye Seo;Woo Taek Kim

作者机构：Department of Systems BiologyDivision of Life ScienceYonsei UniversitySeoul 03722Korea Institute of Life Science and BiotechnologyYonsei UniversitySeoul 03722Korea 

出 版 物：《Journal of Integrative Plant Biology》 (植物学报（英文版）)

年 卷 期：2022年第64卷第3期

页      面：625-631页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 08[工学] 09[农学] 071007[理学-遗传学] 0901[农学-作物学] 0703[理学-化学] 0902[农学-园艺学] 0836[工学-生物工程] 090102[农学-作物遗传育种] 

基　　金：supported by grants from the National Research Foundation(Mid-Career Researcher Program Project No.2017R1A2B2006750 and Basic Science Research Program Project No.2018R1A6A1A03025607) Republic of Korea to Woo T.Kim 

主　　题：Arabidopsis thaliana proteotoxic stress sodium arsenite U-box E3 ligases PUB22/23 26S proteasome complex 

摘      要：The mechanism regulating proteasomal activity under proteotoxic stress conditions remains ***,we showed that arsenite-induced proteotoxic stress resulted in upregulation of Arabidopsis homologous PUB22 and PUB23 U-boxE3 ubiquitin ligases and that pub22 pub23 double mutants displayed arsenite-insensitive seed germination and root growth ***22/PUB23 downregulated 26 S proteasome activity by promoting the dissociation of the 19 S regulatory particle from the holo-proteasome complex,resulting in intracellular accumulation of UbG76 VGFP,an artificial substrate of the proteasome complex,and insoluble poly-ubiquitinated *** results suggest that PUB22/PUB23 play a critical role in arsenite-induced proteotoxic stress response via negative regulation of 26 S proteasome integrity.