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PUB22 and PUB23 U-box E3 ubiquitin ligases negatively regulate 26S proteasome activity under proteotoxic stress conditions 被引量:2
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作者 min yong ahn Dong Hye Seo Woo Taek Kim 《Journal of Integrative Plant Biology》 SCIE CAS CSCD 2022年第3期625-631,共7页
The mechanism regulating proteasomal activity under proteotoxic stress conditions remains unclear.Here,we showed that arsenite-induced proteotoxic stress resulted in upregulation of Arabidopsis homologous PUB22 and PU... The mechanism regulating proteasomal activity under proteotoxic stress conditions remains unclear.Here,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 phenotypes.PUB22/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 proteins.These results suggest that PUB22/PUB23 play a critical role in arsenite-induced proteotoxic stress response via negative regulation of 26 S proteasome integrity. 展开更多
关键词 Arabidopsis thaliana proteotoxic stress sodium arsenite U-box E3 ligases PUB22/23 26S proteasome complex
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