HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis
- Autores
- Mangano, Silvina; Muñoz, Alfonso; Fernández Calvino, Lourdes; Castellano, M. Mar
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Gibberellins (GAs) play important roles in multiple developmental processes and in plant response to the environment. Within the GA pathway, a central regulatory step relies on GA-dependent degradation of the DELLA transcriptional regulators. Nevertheless, the relevance of the stability of other key proteins in this pathway, such as SLY1 and SNE (the F-box proteins involved in DELLA degradation), remains unknown. Here, we take advantage of mutants in the HSP70-HSP90 organizing protein (HOP) co-chaperones and reveal that these proteins contribute to the accumulation of SNE in Arabidopsis. Indeed, HOP proteins, along with HSP90 and HSP70, interact in vivo with SNE, and SNE accumulation is significantly reduced in the hop mutants. Concomitantly, greater accumulation of the DELLA protein RGA is observed in these plants. In agreement with these molecular phenotypes, hop mutants show a hypersensitive response to the GA inhibitor paclobutrazol and display a partial response to the ectopic addition of GA when GA-regulated processes are assayed. These mutants also display different phenotypes associated with alterations in the GA pathway, such as reduced germination rate, delayed bolting, and reduced hypocotyl elongation in response to warm temperatures. Remarkably, ectopic overexpression of SNE reverts the delay in germination and the thermally dependent hypocotyl elongation defect of the hop1 hop2 hop3 mutant, revealing that SNE accumulation is the key aspect of the hop mutant phenotypes. Together, these data reveal a pivotal role for HOP in SNE accumulation and GA signaling.
Fil: Mangano, Silvina. 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. Universidad Politécnica de Madrid; España
Fil: Muñoz, Alfonso. Universidad de Córdoba; España. Universidad Politécnica de Madrid; España
Fil: Fernández Calvino, Lourdes. Universidad Politécnica de Madrid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Castellano, M. Mar. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Madrid; España - Materia
-
HSP70-HSP90 ORGANIZING PROTEIN
PROTEIN FOLDING
PROTEIN STABILITY
RGA
SEED GERMINATION
THERMOMORPHOGENESIS - 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:11336/221916
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/221916 |
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3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in ArabidopsisMangano, SilvinaMuñoz, AlfonsoFernández Calvino, LourdesCastellano, M. MarHSP70-HSP90 ORGANIZING PROTEINPROTEIN FOLDINGPROTEIN STABILITYRGASEED GERMINATIONTHERMOMORPHOGENESIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Gibberellins (GAs) play important roles in multiple developmental processes and in plant response to the environment. Within the GA pathway, a central regulatory step relies on GA-dependent degradation of the DELLA transcriptional regulators. Nevertheless, the relevance of the stability of other key proteins in this pathway, such as SLY1 and SNE (the F-box proteins involved in DELLA degradation), remains unknown. Here, we take advantage of mutants in the HSP70-HSP90 organizing protein (HOP) co-chaperones and reveal that these proteins contribute to the accumulation of SNE in Arabidopsis. Indeed, HOP proteins, along with HSP90 and HSP70, interact in vivo with SNE, and SNE accumulation is significantly reduced in the hop mutants. Concomitantly, greater accumulation of the DELLA protein RGA is observed in these plants. In agreement with these molecular phenotypes, hop mutants show a hypersensitive response to the GA inhibitor paclobutrazol and display a partial response to the ectopic addition of GA when GA-regulated processes are assayed. These mutants also display different phenotypes associated with alterations in the GA pathway, such as reduced germination rate, delayed bolting, and reduced hypocotyl elongation in response to warm temperatures. Remarkably, ectopic overexpression of SNE reverts the delay in germination and the thermally dependent hypocotyl elongation defect of the hop1 hop2 hop3 mutant, revealing that SNE accumulation is the key aspect of the hop mutant phenotypes. Together, these data reveal a pivotal role for HOP in SNE accumulation and GA signaling.Fil: Mangano, Silvina. 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. Universidad Politécnica de Madrid; EspañaFil: Muñoz, Alfonso. Universidad de Córdoba; España. Universidad Politécnica de Madrid; EspañaFil: Fernández Calvino, Lourdes. Universidad Politécnica de Madrid; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Castellano, M. Mar. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Madrid; EspañaCell Press2023-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/221916Mangano, Silvina; Muñoz, Alfonso; Fernández Calvino, Lourdes; Castellano, M. Mar; HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis; Cell Press; Plant Communications; 4; 3; 5-2023; 1-142590-3462CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S2590346223000032info:eu-repo/semantics/altIdentifier/doi/10.1016/j.xplc.2023.100517info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:55:07Zoai:ri.conicet.gov.ar:11336/221916instacron: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 09:55:07.37CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
title |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
spellingShingle |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis Mangano, Silvina HSP70-HSP90 ORGANIZING PROTEIN PROTEIN FOLDING PROTEIN STABILITY RGA SEED GERMINATION THERMOMORPHOGENESIS |
title_short |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
title_full |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
title_fullStr |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
title_full_unstemmed |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
title_sort |
HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis |
dc.creator.none.fl_str_mv |
Mangano, Silvina Muñoz, Alfonso Fernández Calvino, Lourdes Castellano, M. Mar |
author |
Mangano, Silvina |
author_facet |
Mangano, Silvina Muñoz, Alfonso Fernández Calvino, Lourdes Castellano, M. Mar |
author_role |
author |
author2 |
Muñoz, Alfonso Fernández Calvino, Lourdes Castellano, M. Mar |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
HSP70-HSP90 ORGANIZING PROTEIN PROTEIN FOLDING PROTEIN STABILITY RGA SEED GERMINATION THERMOMORPHOGENESIS |
topic |
HSP70-HSP90 ORGANIZING PROTEIN PROTEIN FOLDING PROTEIN STABILITY RGA SEED GERMINATION THERMOMORPHOGENESIS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Gibberellins (GAs) play important roles in multiple developmental processes and in plant response to the environment. Within the GA pathway, a central regulatory step relies on GA-dependent degradation of the DELLA transcriptional regulators. Nevertheless, the relevance of the stability of other key proteins in this pathway, such as SLY1 and SNE (the F-box proteins involved in DELLA degradation), remains unknown. Here, we take advantage of mutants in the HSP70-HSP90 organizing protein (HOP) co-chaperones and reveal that these proteins contribute to the accumulation of SNE in Arabidopsis. Indeed, HOP proteins, along with HSP90 and HSP70, interact in vivo with SNE, and SNE accumulation is significantly reduced in the hop mutants. Concomitantly, greater accumulation of the DELLA protein RGA is observed in these plants. In agreement with these molecular phenotypes, hop mutants show a hypersensitive response to the GA inhibitor paclobutrazol and display a partial response to the ectopic addition of GA when GA-regulated processes are assayed. These mutants also display different phenotypes associated with alterations in the GA pathway, such as reduced germination rate, delayed bolting, and reduced hypocotyl elongation in response to warm temperatures. Remarkably, ectopic overexpression of SNE reverts the delay in germination and the thermally dependent hypocotyl elongation defect of the hop1 hop2 hop3 mutant, revealing that SNE accumulation is the key aspect of the hop mutant phenotypes. Together, these data reveal a pivotal role for HOP in SNE accumulation and GA signaling. Fil: Mangano, Silvina. 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. Universidad Politécnica de Madrid; España Fil: Muñoz, Alfonso. Universidad de Córdoba; España. Universidad Politécnica de Madrid; España Fil: Fernández Calvino, Lourdes. Universidad Politécnica de Madrid; España. Consejo Superior de Investigaciones Científicas; España Fil: Castellano, M. Mar. Consejo Superior de Investigaciones Científicas; España. Universidad Politécnica de Madrid; España |
description |
Gibberellins (GAs) play important roles in multiple developmental processes and in plant response to the environment. Within the GA pathway, a central regulatory step relies on GA-dependent degradation of the DELLA transcriptional regulators. Nevertheless, the relevance of the stability of other key proteins in this pathway, such as SLY1 and SNE (the F-box proteins involved in DELLA degradation), remains unknown. Here, we take advantage of mutants in the HSP70-HSP90 organizing protein (HOP) co-chaperones and reveal that these proteins contribute to the accumulation of SNE in Arabidopsis. Indeed, HOP proteins, along with HSP90 and HSP70, interact in vivo with SNE, and SNE accumulation is significantly reduced in the hop mutants. Concomitantly, greater accumulation of the DELLA protein RGA is observed in these plants. In agreement with these molecular phenotypes, hop mutants show a hypersensitive response to the GA inhibitor paclobutrazol and display a partial response to the ectopic addition of GA when GA-regulated processes are assayed. These mutants also display different phenotypes associated with alterations in the GA pathway, such as reduced germination rate, delayed bolting, and reduced hypocotyl elongation in response to warm temperatures. Remarkably, ectopic overexpression of SNE reverts the delay in germination and the thermally dependent hypocotyl elongation defect of the hop1 hop2 hop3 mutant, revealing that SNE accumulation is the key aspect of the hop mutant phenotypes. Together, these data reveal a pivotal role for HOP in SNE accumulation and GA signaling. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-05 |
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/11336/221916 Mangano, Silvina; Muñoz, Alfonso; Fernández Calvino, Lourdes; Castellano, M. Mar; HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis; Cell Press; Plant Communications; 4; 3; 5-2023; 1-14 2590-3462 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/221916 |
identifier_str_mv |
Mangano, Silvina; Muñoz, Alfonso; Fernández Calvino, Lourdes; Castellano, M. Mar; HOP co-chaperones contribute to GA signaling by promoting the accumulation of the F-box protein SNE in Arabidopsis; Cell Press; Plant Communications; 4; 3; 5-2023; 1-14 2590-3462 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S2590346223000032 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.xplc.2023.100517 |
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 |
Cell Press |
publisher.none.fl_str_mv |
Cell Press |
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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1844613663332237312 |
score |
13.070432 |