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The role of protein phosphatase 2A (PP2A) in the unfolded protein response (UPR) of plants

Protein phosphatase 2A (PP2A) is a key regulator of plant growth and development, but its role in the endoplasmic reticulum (ER) stress response remains elusive. In this study, we investigated the function of PP2A under ER stress using loss-of-function mutants of ROOTS CURL of NAPHTHYLPHTHALAMIC ACI...

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Published in:Biochemical and biophysical research communications 2023-08, Vol.670, p.94-101
Main Authors: Ko, Ki Seong, Yoo, Jae Yong, Vu, Bich Ngoc, Lee, Young Eun, Choi, Ha Na, Lee, Yoo Na, Fanata, Wahyu Indra Duwi, Harmoko, Rikno, Chung, Woo Sik, Hong, Jong Chan, Lee, Kyun Oh
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container_title Biochemical and biophysical research communications
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creator Ko, Ki Seong
Yoo, Jae Yong
Vu, Bich Ngoc
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Chung, Woo Sik
Hong, Jong Chan
Lee, Kyun Oh
description Protein phosphatase 2A (PP2A) is a key regulator of plant growth and development, but its role in the endoplasmic reticulum (ER) stress response remains elusive. In this study, we investigated the function of PP2A under ER stress using loss-of-function mutants of ROOTS CURL of NAPHTHYLPHTHALAMIC ACID1 (RCN1), a regulatory A1 subunit isoform of Arabidopsis PP2A. RCN1 mutants (rcn1-1 and rcn1-2) exhibited reduced sensitivity to tunicamycin (TM), an inhibitor of N-linked glycosylation and inducer of unfolded protein response (UPR) gene expression, resulting in less severe effects compared to wild-type plants (Ws-2 and Col-0). TM negatively impacted PP2A activity in Col-0 plants but did not significantly affect rcn1-2 plants. Additionally, TM treatment did not influence the transcription levels of the PP2AA1(RCN1), 2, and 3 genes in Col-0 plants. Cantharidin, a PP2A inhibitor, exacerbated growth defects in rcn1 plants and alleviated TM-induced growth inhibition in Ws-2 and Col-0 plants. Furthermore, cantharidin treatment mitigated TM hypersensitivity in ire1a&b and bzip28&60 mutants. These findings suggest that PP2A activity is essential for an efficient UPR in Arabidopsis. •PP2A function in ER stress response in plants explored.•rcn1 mutants show reduced sensitivity to ER stress.•PP2A inhibitor cantharidin mitigates plant ER stress.•Findings enhance understanding of UPR signaling pathways.
doi_str_mv 10.1016/j.bbrc.2023.05.106
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These findings suggest that PP2A activity is essential for an efficient UPR in Arabidopsis. •PP2A function in ER stress response in plants explored.•rcn1 mutants show reduced sensitivity to ER stress.•PP2A inhibitor cantharidin mitigates plant ER stress.•Findings enhance understanding of UPR signaling pathways.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2023.05.106</identifier><identifier>PMID: 37290287</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Arabidopsis ; Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Cantharidin ; Cantharidin - pharmacology ; endoplasmic reticulum ; Endoplasmic Reticulum Stress ; ER stress ; gene expression ; Gene Expression Regulation, Plant ; glycosylation ; growth retardation ; hypersensitivity ; loss-of-function mutation ; Mutation ; phosphoprotein phosphatase ; plant growth ; PP2A ; Protein Phosphatase 2 - genetics ; Protein Phosphatase 2 - metabolism ; RCN1 ; stress response ; tunicamycin ; Unfolded Protein Response ; UPR</subject><ispartof>Biochemical and biophysical research communications, 2023-08, Vol.670, p.94-101</ispartof><rights>2023 Elsevier Inc.</rights><rights>Copyright © 2023 Elsevier Inc. 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Yoo, Jae Yong ; Vu, Bich Ngoc ; Lee, Young Eun ; Choi, Ha Na ; Lee, Yoo Na ; Fanata, Wahyu Indra Duwi ; Harmoko, Rikno ; Chung, Woo Sik ; Hong, Jong Chan ; Lee, Kyun Oh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-43f06aa7c726119683287b917f67cfebc0efff0b1cde99e6500b0480a678ffb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Arabidopsis</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Cantharidin</topic><topic>Cantharidin - pharmacology</topic><topic>endoplasmic reticulum</topic><topic>Endoplasmic Reticulum Stress</topic><topic>ER stress</topic><topic>gene expression</topic><topic>Gene Expression Regulation, Plant</topic><topic>glycosylation</topic><topic>growth retardation</topic><topic>hypersensitivity</topic><topic>loss-of-function mutation</topic><topic>Mutation</topic><topic>phosphoprotein phosphatase</topic><topic>plant growth</topic><topic>PP2A</topic><topic>Protein Phosphatase 2 - genetics</topic><topic>Protein Phosphatase 2 - metabolism</topic><topic>RCN1</topic><topic>stress response</topic><topic>tunicamycin</topic><topic>Unfolded Protein Response</topic><topic>UPR</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ko, Ki Seong</creatorcontrib><creatorcontrib>Yoo, Jae Yong</creatorcontrib><creatorcontrib>Vu, Bich Ngoc</creatorcontrib><creatorcontrib>Lee, Young Eun</creatorcontrib><creatorcontrib>Choi, Ha Na</creatorcontrib><creatorcontrib>Lee, Yoo Na</creatorcontrib><creatorcontrib>Fanata, Wahyu Indra Duwi</creatorcontrib><creatorcontrib>Harmoko, Rikno</creatorcontrib><creatorcontrib>Chung, Woo Sik</creatorcontrib><creatorcontrib>Hong, Jong Chan</creatorcontrib><creatorcontrib>Lee, Kyun Oh</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ko, Ki Seong</au><au>Yoo, Jae Yong</au><au>Vu, Bich Ngoc</au><au>Lee, Young Eun</au><au>Choi, Ha Na</au><au>Lee, Yoo Na</au><au>Fanata, Wahyu Indra Duwi</au><au>Harmoko, Rikno</au><au>Chung, Woo Sik</au><au>Hong, Jong Chan</au><au>Lee, Kyun Oh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of protein phosphatase 2A (PP2A) in the unfolded protein response (UPR) of plants</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2023-08-30</date><risdate>2023</risdate><volume>670</volume><spage>94</spage><epage>101</epage><pages>94-101</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Protein phosphatase 2A (PP2A) is a key regulator of plant growth and development, but its role in the endoplasmic reticulum (ER) stress response remains elusive. In this study, we investigated the function of PP2A under ER stress using loss-of-function mutants of ROOTS CURL of NAPHTHYLPHTHALAMIC ACID1 (RCN1), a regulatory A1 subunit isoform of Arabidopsis PP2A. RCN1 mutants (rcn1-1 and rcn1-2) exhibited reduced sensitivity to tunicamycin (TM), an inhibitor of N-linked glycosylation and inducer of unfolded protein response (UPR) gene expression, resulting in less severe effects compared to wild-type plants (Ws-2 and Col-0). TM negatively impacted PP2A activity in Col-0 plants but did not significantly affect rcn1-2 plants. Additionally, TM treatment did not influence the transcription levels of the PP2AA1(RCN1), 2, and 3 genes in Col-0 plants. Cantharidin, a PP2A inhibitor, exacerbated growth defects in rcn1 plants and alleviated TM-induced growth inhibition in Ws-2 and Col-0 plants. Furthermore, cantharidin treatment mitigated TM hypersensitivity in ire1a&amp;b and bzip28&amp;60 mutants. These findings suggest that PP2A activity is essential for an efficient UPR in Arabidopsis. •PP2A function in ER stress response in plants explored.•rcn1 mutants show reduced sensitivity to ER stress.•PP2A inhibitor cantharidin mitigates plant ER stress.•Findings enhance understanding of UPR signaling pathways.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>37290287</pmid><doi>10.1016/j.bbrc.2023.05.106</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-2297-3220</orcidid><orcidid>https://orcid.org/0000-0002-4992-9799</orcidid><orcidid>https://orcid.org/0000-0002-0472-4458</orcidid></addata></record>
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subjects Arabidopsis
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Cantharidin
Cantharidin - pharmacology
endoplasmic reticulum
Endoplasmic Reticulum Stress
ER stress
gene expression
Gene Expression Regulation, Plant
glycosylation
growth retardation
hypersensitivity
loss-of-function mutation
Mutation
phosphoprotein phosphatase
plant growth
PP2A
Protein Phosphatase 2 - genetics
Protein Phosphatase 2 - metabolism
RCN1
stress response
tunicamycin
Unfolded Protein Response
UPR
title The role of protein phosphatase 2A (PP2A) in the unfolded protein response (UPR) of plants
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