Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex

Phytohormone abscisic acid (ABA) regulates key plant development and environmental stress responses. The ubiquitin-proteasome system tightly controls ABA signaling. CULLIN4-RING (CRL4) E3 ubiquitin ligases use the substrate receptor module CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP10)-DDB1-DET1-DDA1 (CDD...

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Detalhes bibliográficos
Autores: Martínez, Cristina, Iniesto, Elisa, García-León, Marta, García-Corredera, Daniel, Fonseca, Sandra, Santiago, César, Yang, Mei, Yu, Renbo, Chen, Haodong, Altmann, Eva, Renatus, Martin, Deng, Xing Wang, Rubio, Vicente
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2024
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/374020
Acesso em linha:http://hdl.handle.net/10261/374020
https://api.elsevier.com/content/abstract/scopus_id/85207349778
Access Level:Acceso aberto
Palavra-chave:ABA receptor
ABA signaling
Arabidopsis
CP: Molecular biology
CP: Plants
CRL4 E3 ligases
CSN
CSN5 inhibitor
DDA1
PYL8
PYR/PYL/RCAR
Plant proteostasis
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spelling Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complexMartínez, CristinaIniesto, ElisaGarcía-León, MartaGarcía-Corredera, DanielFonseca, SandraSantiago, CésarYang, MeiYu, RenboChen, HaodongAltmann, EvaRenatus, MartinDeng, Xing WangRubio, VicenteABA receptorABA signalingArabidopsisCP: Molecular biologyCP: PlantsCRL4 E3 ligasesCSNCSN5 inhibitorDDA1PYL8PYR/PYL/RCARPlant proteostasisPhytohormone abscisic acid (ABA) regulates key plant development and environmental stress responses. The ubiquitin-proteasome system tightly controls ABA signaling. CULLIN4-RING (CRL4) E3 ubiquitin ligases use the substrate receptor module CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP10)-DDB1-DET1-DDA1 (CDDD) to target Arabidopsis ABA receptor PYL8, acting as negative regulators of ABA responses. Conversely, ABA treatment attenuates PYL8 receptor degradation, although the molecular mechanism remained elusive. Here, we show that ABA promotes the disruption of CRL4-CDDD complexes, leading to PYL8 stabilization. ABA-mediated CRL4-CDDD dissociation likely involves an altered association between DDA1-containing complexes and the COP9 signalosome (CSN), a master regulator of the assembly of cullin-based E3 ligases, including CRL4-CDDD. Indeed, treatment with CSN inhibitor CSN5i-3 suppresses the ABA effect on CRL4-CDDD assembly. Our findings indicate that ABA stabilizes PYL8 by altering the dynamics of the CRL4-CDDD-CSN complex association, showing a regulatory mechanism by which a plant hormone inhibits an E3 ubiquitin ligase to protect its own receptors from degradation.Work in V.R.’s laboratory was funded by the Agencia Estatal de Investigación/Fondo Europeo de Desarrollo Regional/European Union (BIO2016-80551-R, PID2019-105495GB-I00, and PID2022-142741NB-I00). E.I., M.G.-L., and D.G.-C. were recipients of FPI fellowships from MINECO and MICINN. S.F. was a recipient of Ramon y Cajal grant RYC-2014-16308 funded by MINECO. V.R. acknowledges financial support from the AEI/ 10.13039/501100011033, through the ‘‘Severo Ochoa’’ program for Centers of Excellence in Research and Development (SEV-2013-0347, SEV-2017-0712, CEX2023-001386-S). X.W.D. acknowledges the support of the Peking University Institute of Advanced Agricultural Sciences, Peking-Tsinghua Center for Life Sciences, and the State Key Laboratory of Protein and Plant GeneResearch.Peer reviewedCell PressAgencia Estatal de Investigación (España)Ministerio de Economía y Competitividad (España)Fonseca, Sandra [0000-0002-2021-4482]Santiago, César [0000-0002-5149-1722]Rubio, Vicente [0000-0002-8800-2400]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/374020https://api.elsevier.com/content/abstract/scopus_id/85207349778reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI//BIO2016-80551-Rinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-105495GB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-142741NB-I00info:eu-repo/grantAgreement/MINECO//RYC-2014-16308info:eu-repo/grantAgreement/MINECO//SEV-2013-0347Cell reportsapplication/pdfhttps://doi.org/10.1016/j.celrep.2024.114802Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3740202026-05-22T06:33:51Z
dc.title.none.fl_str_mv Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
title Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
spellingShingle Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
Martínez, Cristina
ABA receptor
ABA signaling
Arabidopsis
CP: Molecular biology
CP: Plants
CRL4 E3 ligases
CSN
CSN5 inhibitor
DDA1
PYL8
PYR/PYL/RCAR
Plant proteostasis
title_short Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
title_full Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
title_fullStr Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
title_full_unstemmed Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
title_sort Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex
dc.creator.none.fl_str_mv Martínez, Cristina
Iniesto, Elisa
García-León, Marta
García-Corredera, Daniel
Fonseca, Sandra
Santiago, César
Yang, Mei
Yu, Renbo
Chen, Haodong
Altmann, Eva
Renatus, Martin
Deng, Xing Wang
Rubio, Vicente
author Martínez, Cristina
author_facet Martínez, Cristina
Iniesto, Elisa
García-León, Marta
García-Corredera, Daniel
Fonseca, Sandra
Santiago, César
Yang, Mei
Yu, Renbo
Chen, Haodong
Altmann, Eva
Renatus, Martin
Deng, Xing Wang
Rubio, Vicente
author_role author
author2 Iniesto, Elisa
García-León, Marta
García-Corredera, Daniel
Fonseca, Sandra
Santiago, César
Yang, Mei
Yu, Renbo
Chen, Haodong
Altmann, Eva
Renatus, Martin
Deng, Xing Wang
Rubio, Vicente
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Agencia Estatal de Investigación (España)
Ministerio de Economía y Competitividad (España)
Fonseca, Sandra [0000-0002-2021-4482]
Santiago, César [0000-0002-5149-1722]
Rubio, Vicente [0000-0002-8800-2400]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv ABA receptor
ABA signaling
Arabidopsis
CP: Molecular biology
CP: Plants
CRL4 E3 ligases
CSN
CSN5 inhibitor
DDA1
PYL8
PYR/PYL/RCAR
Plant proteostasis
topic ABA receptor
ABA signaling
Arabidopsis
CP: Molecular biology
CP: Plants
CRL4 E3 ligases
CSN
CSN5 inhibitor
DDA1
PYL8
PYR/PYL/RCAR
Plant proteostasis
description Phytohormone abscisic acid (ABA) regulates key plant development and environmental stress responses. The ubiquitin-proteasome system tightly controls ABA signaling. CULLIN4-RING (CRL4) E3 ubiquitin ligases use the substrate receptor module CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP10)-DDB1-DET1-DDA1 (CDDD) to target Arabidopsis ABA receptor PYL8, acting as negative regulators of ABA responses. Conversely, ABA treatment attenuates PYL8 receptor degradation, although the molecular mechanism remained elusive. Here, we show that ABA promotes the disruption of CRL4-CDDD complexes, leading to PYL8 stabilization. ABA-mediated CRL4-CDDD dissociation likely involves an altered association between DDA1-containing complexes and the COP9 signalosome (CSN), a master regulator of the assembly of cullin-based E3 ligases, including CRL4-CDDD. Indeed, treatment with CSN inhibitor CSN5i-3 suppresses the ABA effect on CRL4-CDDD assembly. Our findings indicate that ABA stabilizes PYL8 by altering the dynamics of the CRL4-CDDD-CSN complex association, showing a regulatory mechanism by which a plant hormone inhibits an E3 ubiquitin ligase to protect its own receptors from degradation.
publishDate 2024
dc.date.none.fl_str_mv 2024
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/374020
https://api.elsevier.com/content/abstract/scopus_id/85207349778
url http://hdl.handle.net/10261/374020
https://api.elsevier.com/content/abstract/scopus_id/85207349778
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI//BIO2016-80551-R
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-105495GB-I00
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-142741NB-I00
info:eu-repo/grantAgreement/MINECO//RYC-2014-16308
info:eu-repo/grantAgreement/MINECO//SEV-2013-0347
Cell reports
application/pdf
https://doi.org/10.1016/j.celrep.2024.114802
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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