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

Min Yong Ahn; Dong Hye Seo; Woo Taek Kim

doi:10.1111/jipb.13209

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

Min Yong Ahn, Dong Hye Seo, Woo Taek Kim

Research output: Contribution to journal › Article › peer-review

Abstract

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-box E3 ubiquitin ligases and that pub22pub23 double mutants displayed arsenite-insensitive seed germination and root growth phenotypes. PUB22/PUB23 downregulated 26S proteasome activity by promoting the dissociation of the 19S regulatory particle from the holo-proteasome complex, resulting in intracellular accumulation of Ub^G76V-GFP, 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 26S proteasome integrity.

Original language	English
Pages (from-to)	625-631
Number of pages	7
Journal	Journal of Integrative Plant Biology
Volume	64
Issue number	3
DOIs	https://doi.org/10.1111/jipb.13209
Publication status	Published - 2022 Mar

Bibliographical note

Funding Information:
This work was 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.

Publisher Copyright:
© 2021 Institute of Botany, Chinese Academy of Sciences

All Science Journal Classification (ASJC) codes

Biochemistry
Biochemistry, Genetics and Molecular Biology(all)
Plant Science

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

abstract = "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-box E3 ubiquitin ligases and that pub22pub23 double mutants displayed arsenite-insensitive seed germination and root growth phenotypes. PUB22/PUB23 downregulated 26S proteasome activity by promoting the dissociation of the 19S regulatory particle from the holo-proteasome complex, resulting in intracellular accumulation of UbG76V-GFP, 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 26S proteasome integrity.",

author = "Ahn, {Min Yong} and Seo, {Dong Hye} and Kim, {Woo Taek}",

note = "Funding Information: This work was 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. Publisher Copyright: {\textcopyright} 2021 Institute of Botany, Chinese Academy of Sciences",

year = "2022",

month = mar,

doi = "10.1111/jipb.13209",

language = "English",

volume = "64",

pages = "625--631",

journal = "Acta Botanica Sinica",

issn = "1672-9072",

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AU - Ahn, Min Yong

AU - Seo, Dong Hye

AU - Kim, Woo Taek

N1 - Funding Information: This work was 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. Publisher Copyright: © 2021 Institute of Botany, Chinese Academy of Sciences

PY - 2022/3

Y1 - 2022/3

N2 - 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-box E3 ubiquitin ligases and that pub22pub23 double mutants displayed arsenite-insensitive seed germination and root growth phenotypes. PUB22/PUB23 downregulated 26S proteasome activity by promoting the dissociation of the 19S regulatory particle from the holo-proteasome complex, resulting in intracellular accumulation of UbG76V-GFP, 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 26S proteasome integrity.

AB - 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-box E3 ubiquitin ligases and that pub22pub23 double mutants displayed arsenite-insensitive seed germination and root growth phenotypes. PUB22/PUB23 downregulated 26S proteasome activity by promoting the dissociation of the 19S regulatory particle from the holo-proteasome complex, resulting in intracellular accumulation of UbG76V-GFP, 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 26S proteasome integrity.

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

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