The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants

Autores
Muñoz, Alfonso; Mangano, Silvina; Toribio, René; Fernández Calvino, Lourdes; del Pozo, Juan C.; Castellano, M. Mar
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
HOP (HSP70-HSP90 organising protein) is a conserved family of co-chaperones well known in mammals for its role in the folding of signalling proteins associated with development. In plants, HOP proteins have been involved in the response to multiple stresses, but their role in plant development remains elusive. Herein, we describe that the members of the HOP family participate in different aspects of plant development as well as in the response to warm temperatures through the regulation of auxin signalling. Arabidopsis hop1 hop2 hop3 triple mutant shows different auxin-related phenotypes and a reduced auxin sensitivity. HOP interacts with TIR1 auxin coreceptor in vivo. Furthermore, TIR1 accumulation and auxin transcriptional response are reduced in the hop1 hop2 hop3 triple mutant, suggesting that HOP's function in auxin signalling is related, at least, to TIR1 interaction and stabilisation. Interestingly, HOP proteins form part of the same complexes as SGT1b (a different HSP90 co-chaperone) and these co-chaperones synergistically cooperate in auxin signalling. This study provides relevant data about the role of HOP in auxin regulation in plants and uncovers that both co-chaperones, SGT1b and HOP, cooperate in the stabilisation of common targets involved in plant development.
Fil: Muñoz, Alfonso. Universidad Politécnica de Madrid; España. Universidad de Córdoba; España
Fil: Mangano, Silvina. Universidad Politécnica de Madrid; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Toribio, René. Universidad Politécnica de Madrid; España
Fil: Fernández Calvino, Lourdes. Universidad Politécnica de Madrid; España
Fil: del Pozo, Juan C.. Universidad Politécnica de Madrid; España
Fil: Castellano, M. Mar. Universidad Politécnica de Madrid; España
Materia
ARABIDOPSIS THALIANA
AUXIN CORECEPTORS
AUXIN SIGNALLING
HSP70-HSP90 ORGANIZING PROTEIN
HSP90 CO-CHAPERONES
SGT1B
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/214018
Acceder
id CONICETDig_99750f99552edb55148f75aaa6f537d8
oai_identifier_str oai:ri.conicet.gov.ar:11336/214018
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plantsMuñoz, AlfonsoMangano, SilvinaToribio, RenéFernández Calvino, Lourdesdel Pozo, Juan C.Castellano, M. MarARABIDOPSIS THALIANAAUXIN CORECEPTORSAUXIN SIGNALLINGHSP70-HSP90 ORGANIZING PROTEINHSP90 CO-CHAPERONESSGT1Bhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1HOP (HSP70-HSP90 organising protein) is a conserved family of co-chaperones well known in mammals for its role in the folding of signalling proteins associated with development. In plants, HOP proteins have been involved in the response to multiple stresses, but their role in plant development remains elusive. Herein, we describe that the members of the HOP family participate in different aspects of plant development as well as in the response to warm temperatures through the regulation of auxin signalling. Arabidopsis hop1 hop2 hop3 triple mutant shows different auxin-related phenotypes and a reduced auxin sensitivity. HOP interacts with TIR1 auxin coreceptor in vivo. Furthermore, TIR1 accumulation and auxin transcriptional response are reduced in the hop1 hop2 hop3 triple mutant, suggesting that HOP's function in auxin signalling is related, at least, to TIR1 interaction and stabilisation. Interestingly, HOP proteins form part of the same complexes as SGT1b (a different HSP90 co-chaperone) and these co-chaperones synergistically cooperate in auxin signalling. This study provides relevant data about the role of HOP in auxin regulation in plants and uncovers that both co-chaperones, SGT1b and HOP, cooperate in the stabilisation of common targets involved in plant development.Fil: Muñoz, Alfonso. Universidad Politécnica de Madrid; España. Universidad de Córdoba; EspañaFil: Mangano, Silvina. Universidad Politécnica de Madrid; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Toribio, René. Universidad Politécnica de Madrid; EspañaFil: Fernández Calvino, Lourdes. Universidad Politécnica de Madrid; EspañaFil: del Pozo, Juan C.. Universidad Politécnica de Madrid; EspañaFil: Castellano, M. Mar. Universidad Politécnica de Madrid; EspañaWiley Blackwell Publishing, Inc2022-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/214018Muñoz, Alfonso; Mangano, Silvina; Toribio, René; Fernández Calvino, Lourdes; del Pozo, Juan C.; et al.; The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants; Wiley Blackwell Publishing, Inc; Plant, Cell and Environment; 45; 8; 8-2022; 2508-25190140-7791CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/pce.14366info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:32:22Zoai:ri.conicet.gov.ar:11336/214018instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:32:22.343CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
title The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
spellingShingle The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
Muñoz, Alfonso
ARABIDOPSIS THALIANA
AUXIN CORECEPTORS
AUXIN SIGNALLING
HSP70-HSP90 ORGANIZING PROTEIN
HSP90 CO-CHAPERONES
SGT1B
title_short The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
title_full The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
title_fullStr The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
title_full_unstemmed The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
title_sort The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants
dc.creator.none.fl_str_mv Muñoz, Alfonso
Mangano, Silvina
Toribio, René
Fernández Calvino, Lourdes
del Pozo, Juan C.
Castellano, M. Mar
author Muñoz, Alfonso
author_facet Muñoz, Alfonso
Mangano, Silvina
Toribio, René
Fernández Calvino, Lourdes
del Pozo, Juan C.
Castellano, M. Mar
author_role author
author2 Mangano, Silvina
Toribio, René
Fernández Calvino, Lourdes
del Pozo, Juan C.
Castellano, M. Mar
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ARABIDOPSIS THALIANA
AUXIN CORECEPTORS
AUXIN SIGNALLING
HSP70-HSP90 ORGANIZING PROTEIN
HSP90 CO-CHAPERONES
SGT1B
topic ARABIDOPSIS THALIANA
AUXIN CORECEPTORS
AUXIN SIGNALLING
HSP70-HSP90 ORGANIZING PROTEIN
HSP90 CO-CHAPERONES
SGT1B
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv HOP (HSP70-HSP90 organising protein) is a conserved family of co-chaperones well known in mammals for its role in the folding of signalling proteins associated with development. In plants, HOP proteins have been involved in the response to multiple stresses, but their role in plant development remains elusive. Herein, we describe that the members of the HOP family participate in different aspects of plant development as well as in the response to warm temperatures through the regulation of auxin signalling. Arabidopsis hop1 hop2 hop3 triple mutant shows different auxin-related phenotypes and a reduced auxin sensitivity. HOP interacts with TIR1 auxin coreceptor in vivo. Furthermore, TIR1 accumulation and auxin transcriptional response are reduced in the hop1 hop2 hop3 triple mutant, suggesting that HOP's function in auxin signalling is related, at least, to TIR1 interaction and stabilisation. Interestingly, HOP proteins form part of the same complexes as SGT1b (a different HSP90 co-chaperone) and these co-chaperones synergistically cooperate in auxin signalling. This study provides relevant data about the role of HOP in auxin regulation in plants and uncovers that both co-chaperones, SGT1b and HOP, cooperate in the stabilisation of common targets involved in plant development.
Fil: Muñoz, Alfonso. Universidad Politécnica de Madrid; España. Universidad de Córdoba; España
Fil: Mangano, Silvina. Universidad Politécnica de Madrid; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Toribio, René. Universidad Politécnica de Madrid; España
Fil: Fernández Calvino, Lourdes. Universidad Politécnica de Madrid; España
Fil: del Pozo, Juan C.. Universidad Politécnica de Madrid; España
Fil: Castellano, M. Mar. Universidad Politécnica de Madrid; España
description HOP (HSP70-HSP90 organising protein) is a conserved family of co-chaperones well known in mammals for its role in the folding of signalling proteins associated with development. In plants, HOP proteins have been involved in the response to multiple stresses, but their role in plant development remains elusive. Herein, we describe that the members of the HOP family participate in different aspects of plant development as well as in the response to warm temperatures through the regulation of auxin signalling. Arabidopsis hop1 hop2 hop3 triple mutant shows different auxin-related phenotypes and a reduced auxin sensitivity. HOP interacts with TIR1 auxin coreceptor in vivo. Furthermore, TIR1 accumulation and auxin transcriptional response are reduced in the hop1 hop2 hop3 triple mutant, suggesting that HOP's function in auxin signalling is related, at least, to TIR1 interaction and stabilisation. Interestingly, HOP proteins form part of the same complexes as SGT1b (a different HSP90 co-chaperone) and these co-chaperones synergistically cooperate in auxin signalling. This study provides relevant data about the role of HOP in auxin regulation in plants and uncovers that both co-chaperones, SGT1b and HOP, cooperate in the stabilisation of common targets involved in plant development.
publishDate 2022
dc.date.none.fl_str_mv 2022-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/214018
Muñoz, Alfonso; Mangano, Silvina; Toribio, René; Fernández Calvino, Lourdes; del Pozo, Juan C.; et al.; The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants; Wiley Blackwell Publishing, Inc; Plant, Cell and Environment; 45; 8; 8-2022; 2508-2519
0140-7791
CONICET Digital
CONICET
url http://hdl.handle.net/11336/214018
identifier_str_mv Muñoz, Alfonso; Mangano, Silvina; Toribio, René; Fernández Calvino, Lourdes; del Pozo, Juan C.; et al.; The co-chaperone HOP participates in TIR1 stabilisation and in auxin response in plants; Wiley Blackwell Publishing, Inc; Plant, Cell and Environment; 45; 8; 8-2022; 2508-2519
0140-7791
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/pce.14366
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.069144

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