Arabidopsis ERdj3B coordinates with ERECTA-family receptor kinases to regulate ovule development and the heat stress response

The endoplasmic reticulum-localized DnaJ family 3B (ERdj3B), is a component of the stromal cell-derived factor 2 (SDF2)-ERdj3B-binding immunoglobulin protein (BiP) chaperone complex, which functions in protein folding, translocation, and quality control. We found that ERdj3B mutations affected integ...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Plant cell 2022-09, Vol.34 (10), p.3665-3684
Hauptverfasser: Leng, Ya-Jun, Yao, Ya-Sen, Yang, Ke-Zhen, Wu, Pei-Xiang, Xia, Yu-Xin, Zuo, Chao-Ran, Luo, Jing-Hong, Wang, Pu, Liu, Yang-Yang, Zhang, Xue-Qin, Ye, De, Le, Jie, Chen, Li-Qun
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 3684
container_issue 10
container_start_page 3665
container_title The Plant cell
container_volume 34
creator Leng, Ya-Jun
Yao, Ya-Sen
Yang, Ke-Zhen
Wu, Pei-Xiang
Xia, Yu-Xin
Zuo, Chao-Ran
Luo, Jing-Hong
Wang, Pu
Liu, Yang-Yang
Zhang, Xue-Qin
Ye, De
Le, Jie
Chen, Li-Qun
description The endoplasmic reticulum-localized DnaJ family 3B (ERdj3B), is a component of the stromal cell-derived factor 2 (SDF2)-ERdj3B-binding immunoglobulin protein (BiP) chaperone complex, which functions in protein folding, translocation, and quality control. We found that ERdj3B mutations affected integument development in the Ler ecotype but not in the Col-0 ecotype of Arabidopsis (Arabidopsis thaliana). Map-based cloning identified the ERECTA (ER) gene as a natural modifier of ERdj3B. The double mutation of ERdj3B and ER caused a major defect in the inner integument under heat stress. Additional mutation of the ER paralog ERECTA-LIKE 1 (ERL1) or ERL2 to the erdj3b er double mutant exacerbated the defective integument phenotype. The double mutation of ER and SDF2, the other component of the SDF2-ERdj3B-BiP complex, resulted in similar defects in the inner integument. Furthermore, both the protein abundance and plasma membrane partitioning of ER, ERL1, and ERL2 were markedly reduced in erdj3b plants, indicating that the SDF2-ERdj3B-BiP chaperone complex might control the translocation of ERECTA-family proteins from the endoplasmic reticulum to the plasma membrane. Our results suggest that the SDF2-ERdj3B-BiP complex functions in ovule development and the heat stress response in coordination with ERECTA-family receptor kinases.
doi_str_mv 10.1093/plcell/koac226
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9516030</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2696006769</sourcerecordid><originalsourceid>FETCH-LOGICAL-c390t-aeed0250c85464f0648415b0887c0582908d2a22a07c17890d061904161bfb553</originalsourceid><addsrcrecordid>eNpVkUFr3DAQhU1paNK01x6Ljr04GcmWLF0K22XbFAKBkkJvQpbGWSe25Uryhhz636uwm5CcZpj55s0wryg-UTijoKrzebA4DOd33ljGxJvihPKKlUzJP29zDjWUteD0uHgf4y0A0Iaqd8VxxaVqaC1Oin-rYNre-Tn2kWx-udvqG7HeB9dPJmEk933a5vpmfb0qOzP2wwMJaHFOPpC7zMTMJJ9rN8uQB4jfLQMShzsc_DzilIiZHElbJFs0icQUMMaMx9lPET8UR50ZIn48xNPi9_fN9fqivLz68XO9uixtpSCVBtEB42Alr0XdgahlTXkLUjYWuGQKpGOGMQONpY1U4EBQBTUVtO1azqvT4uted17aEZ3NdwUz6Dn0owkP2ptev-5M_Vbf-J1WnAqoIAt8OQgE_3fBmPTYx8fPmwn9EjUTSgCIRqiMnu1RG3yMAbvnNRT0o2d675k-eJYHPr887hl_Mqn6Dx59lvY</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2696006769</pqid></control><display><type>article</type><title>Arabidopsis ERdj3B coordinates with ERECTA-family receptor kinases to regulate ovule development and the heat stress response</title><source>MEDLINE</source><source>EZB Free E-Journals</source><source>Oxford Journals</source><creator>Leng, Ya-Jun ; Yao, Ya-Sen ; Yang, Ke-Zhen ; Wu, Pei-Xiang ; Xia, Yu-Xin ; Zuo, Chao-Ran ; Luo, Jing-Hong ; Wang, Pu ; Liu, Yang-Yang ; Zhang, Xue-Qin ; Ye, De ; Le, Jie ; Chen, Li-Qun</creator><creatorcontrib>Leng, Ya-Jun ; Yao, Ya-Sen ; Yang, Ke-Zhen ; Wu, Pei-Xiang ; Xia, Yu-Xin ; Zuo, Chao-Ran ; Luo, Jing-Hong ; Wang, Pu ; Liu, Yang-Yang ; Zhang, Xue-Qin ; Ye, De ; Le, Jie ; Chen, Li-Qun</creatorcontrib><description>The endoplasmic reticulum-localized DnaJ family 3B (ERdj3B), is a component of the stromal cell-derived factor 2 (SDF2)-ERdj3B-binding immunoglobulin protein (BiP) chaperone complex, which functions in protein folding, translocation, and quality control. We found that ERdj3B mutations affected integument development in the Ler ecotype but not in the Col-0 ecotype of Arabidopsis (Arabidopsis thaliana). Map-based cloning identified the ERECTA (ER) gene as a natural modifier of ERdj3B. The double mutation of ERdj3B and ER caused a major defect in the inner integument under heat stress. Additional mutation of the ER paralog ERECTA-LIKE 1 (ERL1) or ERL2 to the erdj3b er double mutant exacerbated the defective integument phenotype. The double mutation of ER and SDF2, the other component of the SDF2-ERdj3B-BiP complex, resulted in similar defects in the inner integument. Furthermore, both the protein abundance and plasma membrane partitioning of ER, ERL1, and ERL2 were markedly reduced in erdj3b plants, indicating that the SDF2-ERdj3B-BiP chaperone complex might control the translocation of ERECTA-family proteins from the endoplasmic reticulum to the plasma membrane. Our results suggest that the SDF2-ERdj3B-BiP complex functions in ovule development and the heat stress response in coordination with ERECTA-family receptor kinases.</description><identifier>ISSN: 1040-4651</identifier><identifier>EISSN: 1532-298X</identifier><identifier>DOI: 10.1093/plcell/koac226</identifier><identifier>PMID: 35897146</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Carrier Proteins - metabolism ; Heat-Shock Response ; HSP40 Heat-Shock Proteins - metabolism ; Ovule - metabolism ; Protein Serine-Threonine Kinases</subject><ispartof>The Plant cell, 2022-09, Vol.34 (10), p.3665-3684</ispartof><rights>American Society of Plant Biologists 2022. All rights reserved. For permissions, please email: journals.permissions@oup.com.</rights><rights>American Society of Plant Biologists 2022. All rights reserved. For permissions, please email: journals.permissions@oup.com 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-aeed0250c85464f0648415b0887c0582908d2a22a07c17890d061904161bfb553</citedby><cites>FETCH-LOGICAL-c390t-aeed0250c85464f0648415b0887c0582908d2a22a07c17890d061904161bfb553</cites><orcidid>0000-0002-8698-210X ; 0000-0001-9167-4331 ; 0000-0001-9621-8837 ; 0000-0001-8854-3031 ; 0000-0001-7053-1083 ; 0000-0001-5958-6972 ; 0000-0003-4953-1809 ; 0000-0002-9875-3339 ; 0000-0002-8179-6172 ; 0000-0002-6775-8946 ; 0000-0002-4346-1451 ; 0000-0001-8291-3273 ; 0000-0003-1988-3598</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35897146$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leng, Ya-Jun</creatorcontrib><creatorcontrib>Yao, Ya-Sen</creatorcontrib><creatorcontrib>Yang, Ke-Zhen</creatorcontrib><creatorcontrib>Wu, Pei-Xiang</creatorcontrib><creatorcontrib>Xia, Yu-Xin</creatorcontrib><creatorcontrib>Zuo, Chao-Ran</creatorcontrib><creatorcontrib>Luo, Jing-Hong</creatorcontrib><creatorcontrib>Wang, Pu</creatorcontrib><creatorcontrib>Liu, Yang-Yang</creatorcontrib><creatorcontrib>Zhang, Xue-Qin</creatorcontrib><creatorcontrib>Ye, De</creatorcontrib><creatorcontrib>Le, Jie</creatorcontrib><creatorcontrib>Chen, Li-Qun</creatorcontrib><title>Arabidopsis ERdj3B coordinates with ERECTA-family receptor kinases to regulate ovule development and the heat stress response</title><title>The Plant cell</title><addtitle>Plant Cell</addtitle><description>The endoplasmic reticulum-localized DnaJ family 3B (ERdj3B), is a component of the stromal cell-derived factor 2 (SDF2)-ERdj3B-binding immunoglobulin protein (BiP) chaperone complex, which functions in protein folding, translocation, and quality control. We found that ERdj3B mutations affected integument development in the Ler ecotype but not in the Col-0 ecotype of Arabidopsis (Arabidopsis thaliana). Map-based cloning identified the ERECTA (ER) gene as a natural modifier of ERdj3B. The double mutation of ERdj3B and ER caused a major defect in the inner integument under heat stress. Additional mutation of the ER paralog ERECTA-LIKE 1 (ERL1) or ERL2 to the erdj3b er double mutant exacerbated the defective integument phenotype. The double mutation of ER and SDF2, the other component of the SDF2-ERdj3B-BiP complex, resulted in similar defects in the inner integument. Furthermore, both the protein abundance and plasma membrane partitioning of ER, ERL1, and ERL2 were markedly reduced in erdj3b plants, indicating that the SDF2-ERdj3B-BiP chaperone complex might control the translocation of ERECTA-family proteins from the endoplasmic reticulum to the plasma membrane. Our results suggest that the SDF2-ERdj3B-BiP complex functions in ovule development and the heat stress response in coordination with ERECTA-family receptor kinases.</description><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Carrier Proteins - metabolism</subject><subject>Heat-Shock Response</subject><subject>HSP40 Heat-Shock Proteins - metabolism</subject><subject>Ovule - metabolism</subject><subject>Protein Serine-Threonine Kinases</subject><issn>1040-4651</issn><issn>1532-298X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUFr3DAQhU1paNK01x6Ljr04GcmWLF0K22XbFAKBkkJvQpbGWSe25Uryhhz636uwm5CcZpj55s0wryg-UTijoKrzebA4DOd33ljGxJvihPKKlUzJP29zDjWUteD0uHgf4y0A0Iaqd8VxxaVqaC1Oin-rYNre-Tn2kWx-udvqG7HeB9dPJmEk933a5vpmfb0qOzP2wwMJaHFOPpC7zMTMJJ9rN8uQB4jfLQMShzsc_DzilIiZHElbJFs0icQUMMaMx9lPET8UR50ZIn48xNPi9_fN9fqivLz68XO9uixtpSCVBtEB42Alr0XdgahlTXkLUjYWuGQKpGOGMQONpY1U4EBQBTUVtO1azqvT4uted17aEZ3NdwUz6Dn0owkP2ptev-5M_Vbf-J1WnAqoIAt8OQgE_3fBmPTYx8fPmwn9EjUTSgCIRqiMnu1RG3yMAbvnNRT0o2d675k-eJYHPr887hl_Mqn6Dx59lvY</recordid><startdate>20220927</startdate><enddate>20220927</enddate><creator>Leng, Ya-Jun</creator><creator>Yao, Ya-Sen</creator><creator>Yang, Ke-Zhen</creator><creator>Wu, Pei-Xiang</creator><creator>Xia, Yu-Xin</creator><creator>Zuo, Chao-Ran</creator><creator>Luo, Jing-Hong</creator><creator>Wang, Pu</creator><creator>Liu, Yang-Yang</creator><creator>Zhang, Xue-Qin</creator><creator>Ye, De</creator><creator>Le, Jie</creator><creator>Chen, Li-Qun</creator><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8698-210X</orcidid><orcidid>https://orcid.org/0000-0001-9167-4331</orcidid><orcidid>https://orcid.org/0000-0001-9621-8837</orcidid><orcidid>https://orcid.org/0000-0001-8854-3031</orcidid><orcidid>https://orcid.org/0000-0001-7053-1083</orcidid><orcidid>https://orcid.org/0000-0001-5958-6972</orcidid><orcidid>https://orcid.org/0000-0003-4953-1809</orcidid><orcidid>https://orcid.org/0000-0002-9875-3339</orcidid><orcidid>https://orcid.org/0000-0002-8179-6172</orcidid><orcidid>https://orcid.org/0000-0002-6775-8946</orcidid><orcidid>https://orcid.org/0000-0002-4346-1451</orcidid><orcidid>https://orcid.org/0000-0001-8291-3273</orcidid><orcidid>https://orcid.org/0000-0003-1988-3598</orcidid></search><sort><creationdate>20220927</creationdate><title>Arabidopsis ERdj3B coordinates with ERECTA-family receptor kinases to regulate ovule development and the heat stress response</title><author>Leng, Ya-Jun ; Yao, Ya-Sen ; Yang, Ke-Zhen ; Wu, Pei-Xiang ; Xia, Yu-Xin ; Zuo, Chao-Ran ; Luo, Jing-Hong ; Wang, Pu ; Liu, Yang-Yang ; Zhang, Xue-Qin ; Ye, De ; Le, Jie ; Chen, Li-Qun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-aeed0250c85464f0648415b0887c0582908d2a22a07c17890d061904161bfb553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Carrier Proteins - metabolism</topic><topic>Heat-Shock Response</topic><topic>HSP40 Heat-Shock Proteins - metabolism</topic><topic>Ovule - metabolism</topic><topic>Protein Serine-Threonine Kinases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leng, Ya-Jun</creatorcontrib><creatorcontrib>Yao, Ya-Sen</creatorcontrib><creatorcontrib>Yang, Ke-Zhen</creatorcontrib><creatorcontrib>Wu, Pei-Xiang</creatorcontrib><creatorcontrib>Xia, Yu-Xin</creatorcontrib><creatorcontrib>Zuo, Chao-Ran</creatorcontrib><creatorcontrib>Luo, Jing-Hong</creatorcontrib><creatorcontrib>Wang, Pu</creatorcontrib><creatorcontrib>Liu, Yang-Yang</creatorcontrib><creatorcontrib>Zhang, Xue-Qin</creatorcontrib><creatorcontrib>Ye, De</creatorcontrib><creatorcontrib>Le, Jie</creatorcontrib><creatorcontrib>Chen, Li-Qun</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>PubMed Central (Full Participant titles)</collection><jtitle>The Plant cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leng, Ya-Jun</au><au>Yao, Ya-Sen</au><au>Yang, Ke-Zhen</au><au>Wu, Pei-Xiang</au><au>Xia, Yu-Xin</au><au>Zuo, Chao-Ran</au><au>Luo, Jing-Hong</au><au>Wang, Pu</au><au>Liu, Yang-Yang</au><au>Zhang, Xue-Qin</au><au>Ye, De</au><au>Le, Jie</au><au>Chen, Li-Qun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arabidopsis ERdj3B coordinates with ERECTA-family receptor kinases to regulate ovule development and the heat stress response</atitle><jtitle>The Plant cell</jtitle><addtitle>Plant Cell</addtitle><date>2022-09-27</date><risdate>2022</risdate><volume>34</volume><issue>10</issue><spage>3665</spage><epage>3684</epage><pages>3665-3684</pages><issn>1040-4651</issn><eissn>1532-298X</eissn><abstract>The endoplasmic reticulum-localized DnaJ family 3B (ERdj3B), is a component of the stromal cell-derived factor 2 (SDF2)-ERdj3B-binding immunoglobulin protein (BiP) chaperone complex, which functions in protein folding, translocation, and quality control. We found that ERdj3B mutations affected integument development in the Ler ecotype but not in the Col-0 ecotype of Arabidopsis (Arabidopsis thaliana). Map-based cloning identified the ERECTA (ER) gene as a natural modifier of ERdj3B. The double mutation of ERdj3B and ER caused a major defect in the inner integument under heat stress. Additional mutation of the ER paralog ERECTA-LIKE 1 (ERL1) or ERL2 to the erdj3b er double mutant exacerbated the defective integument phenotype. The double mutation of ER and SDF2, the other component of the SDF2-ERdj3B-BiP complex, resulted in similar defects in the inner integument. Furthermore, both the protein abundance and plasma membrane partitioning of ER, ERL1, and ERL2 were markedly reduced in erdj3b plants, indicating that the SDF2-ERdj3B-BiP chaperone complex might control the translocation of ERECTA-family proteins from the endoplasmic reticulum to the plasma membrane. Our results suggest that the SDF2-ERdj3B-BiP complex functions in ovule development and the heat stress response in coordination with ERECTA-family receptor kinases.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>35897146</pmid><doi>10.1093/plcell/koac226</doi><tpages>20</tpages><orcidid>https://orcid.org/0000-0002-8698-210X</orcidid><orcidid>https://orcid.org/0000-0001-9167-4331</orcidid><orcidid>https://orcid.org/0000-0001-9621-8837</orcidid><orcidid>https://orcid.org/0000-0001-8854-3031</orcidid><orcidid>https://orcid.org/0000-0001-7053-1083</orcidid><orcidid>https://orcid.org/0000-0001-5958-6972</orcidid><orcidid>https://orcid.org/0000-0003-4953-1809</orcidid><orcidid>https://orcid.org/0000-0002-9875-3339</orcidid><orcidid>https://orcid.org/0000-0002-8179-6172</orcidid><orcidid>https://orcid.org/0000-0002-6775-8946</orcidid><orcidid>https://orcid.org/0000-0002-4346-1451</orcidid><orcidid>https://orcid.org/0000-0001-8291-3273</orcidid><orcidid>https://orcid.org/0000-0003-1988-3598</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1040-4651
ispartof The Plant cell, 2022-09, Vol.34 (10), p.3665-3684
issn 1040-4651
1532-298X
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9516030
source MEDLINE; EZB Free E-Journals; Oxford Journals
subjects Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Carrier Proteins - metabolism
Heat-Shock Response
HSP40 Heat-Shock Proteins - metabolism
Ovule - metabolism
Protein Serine-Threonine Kinases
title Arabidopsis ERdj3B coordinates with ERECTA-family receptor kinases to regulate ovule development and the heat stress response
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T06%3A55%3A52IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Arabidopsis%20ERdj3B%20coordinates%20with%20ERECTA-family%20receptor%20kinases%20to%20regulate%20ovule%20development%20and%20the%20heat%20stress%20response&rft.jtitle=The%20Plant%20cell&rft.au=Leng,%20Ya-Jun&rft.date=2022-09-27&rft.volume=34&rft.issue=10&rft.spage=3665&rft.epage=3684&rft.pages=3665-3684&rft.issn=1040-4651&rft.eissn=1532-298X&rft_id=info:doi/10.1093/plcell/koac226&rft_dat=%3Cproquest_pubme%3E2696006769%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2696006769&rft_id=info:pmid/35897146&rfr_iscdi=true