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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/214018
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oai:ri.conicet.gov.ar:11336/214018 |
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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 Técnicas2025-09-03T09:43:17Zoai: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:34982025-09-03 09:43:18.153CONICET 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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1842268592393945088 |
score |
13.13397 |