HOP, a Co-chaperone Involved in Response to Stress in Plants
- Autores
- Toribio, René; Mangano, Silvina; Fernández Bautista, Nuria; Muñoz, Alfonso; Castellano, M. Mar
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Protein folding is an essential step for protein functionality. In eukaryotes this process is carried out by multiple chaperones that act in a cooperative manner to maintain the proteome homeostasis. Some of these chaperones are assisted during protein folding by different co-chaperones. One of these co-chaperones is HOP, the HSP70-HSP90 organizing protein. This assistant protein, due to its importance, has been deeply analyzed in other eukaryotes, but its function has only recently started to be envisaged in plants. In this kingdom, the role of HOP has been associated to plant response to different cellular, biotic and abiotic stresses. In this article, we analyze the current knowledge about HOP in eukaryotes, paying a special attention to the recently described roles of HOP in plants. In addition, we discuss the recent breakthroughs in the field and the possible new avenues for the study of plant HOP proteins in the future.
Fil: Toribio, René. Universidad Politécnica de Madrid; 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: Fernández Bautista, Nuria. Universidad Politécnica de Madrid; España
Fil: Muñoz, Alfonso. Universidad de Córdoba; España
Fil: Castellano, M. Mar. Universidad Politécnica de Madrid; España - Materia
-
CO-CHAPERONE
HOP
HSP70
HSP90
PROTEIN FOLDING
QUALITY CONTROL - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/211435
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HOP, a Co-chaperone Involved in Response to Stress in PlantsToribio, RenéMangano, SilvinaFernández Bautista, NuriaMuñoz, AlfonsoCastellano, M. MarCO-CHAPERONEHOPHSP70HSP90PROTEIN FOLDINGQUALITY CONTROLhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Protein folding is an essential step for protein functionality. In eukaryotes this process is carried out by multiple chaperones that act in a cooperative manner to maintain the proteome homeostasis. Some of these chaperones are assisted during protein folding by different co-chaperones. One of these co-chaperones is HOP, the HSP70-HSP90 organizing protein. This assistant protein, due to its importance, has been deeply analyzed in other eukaryotes, but its function has only recently started to be envisaged in plants. In this kingdom, the role of HOP has been associated to plant response to different cellular, biotic and abiotic stresses. In this article, we analyze the current knowledge about HOP in eukaryotes, paying a special attention to the recently described roles of HOP in plants. In addition, we discuss the recent breakthroughs in the field and the possible new avenues for the study of plant HOP proteins in the future.Fil: Toribio, René. Universidad Politécnica de Madrid; 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: Fernández Bautista, Nuria. Universidad Politécnica de Madrid; EspañaFil: Muñoz, Alfonso. Universidad de Córdoba; EspañaFil: Castellano, M. Mar. Universidad Politécnica de Madrid; EspañaFrontiers Media2020-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/211435Toribio, René; Mangano, Silvina; Fernández Bautista, Nuria; Muñoz, Alfonso; Castellano, M. Mar; HOP, a Co-chaperone Involved in Response to Stress in Plants; Frontiers Media; Frontiers in Plant Science; 11; 10-2020; 1-81664-462XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2020.591940info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:56:10Zoai:ri.conicet.gov.ar:11336/211435instacron: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 09:56:10.461CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
title |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
spellingShingle |
HOP, a Co-chaperone Involved in Response to Stress in Plants Toribio, René CO-CHAPERONE HOP HSP70 HSP90 PROTEIN FOLDING QUALITY CONTROL |
title_short |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
title_full |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
title_fullStr |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
title_full_unstemmed |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
title_sort |
HOP, a Co-chaperone Involved in Response to Stress in Plants |
dc.creator.none.fl_str_mv |
Toribio, René Mangano, Silvina Fernández Bautista, Nuria Muñoz, Alfonso Castellano, M. Mar |
author |
Toribio, René |
author_facet |
Toribio, René Mangano, Silvina Fernández Bautista, Nuria Muñoz, Alfonso Castellano, M. Mar |
author_role |
author |
author2 |
Mangano, Silvina Fernández Bautista, Nuria Muñoz, Alfonso Castellano, M. Mar |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
CO-CHAPERONE HOP HSP70 HSP90 PROTEIN FOLDING QUALITY CONTROL |
topic |
CO-CHAPERONE HOP HSP70 HSP90 PROTEIN FOLDING QUALITY CONTROL |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Protein folding is an essential step for protein functionality. In eukaryotes this process is carried out by multiple chaperones that act in a cooperative manner to maintain the proteome homeostasis. Some of these chaperones are assisted during protein folding by different co-chaperones. One of these co-chaperones is HOP, the HSP70-HSP90 organizing protein. This assistant protein, due to its importance, has been deeply analyzed in other eukaryotes, but its function has only recently started to be envisaged in plants. In this kingdom, the role of HOP has been associated to plant response to different cellular, biotic and abiotic stresses. In this article, we analyze the current knowledge about HOP in eukaryotes, paying a special attention to the recently described roles of HOP in plants. In addition, we discuss the recent breakthroughs in the field and the possible new avenues for the study of plant HOP proteins in the future. Fil: Toribio, René. Universidad Politécnica de Madrid; 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: Fernández Bautista, Nuria. Universidad Politécnica de Madrid; España Fil: Muñoz, Alfonso. Universidad de Córdoba; España Fil: Castellano, M. Mar. Universidad Politécnica de Madrid; España |
description |
Protein folding is an essential step for protein functionality. In eukaryotes this process is carried out by multiple chaperones that act in a cooperative manner to maintain the proteome homeostasis. Some of these chaperones are assisted during protein folding by different co-chaperones. One of these co-chaperones is HOP, the HSP70-HSP90 organizing protein. This assistant protein, due to its importance, has been deeply analyzed in other eukaryotes, but its function has only recently started to be envisaged in plants. In this kingdom, the role of HOP has been associated to plant response to different cellular, biotic and abiotic stresses. In this article, we analyze the current knowledge about HOP in eukaryotes, paying a special attention to the recently described roles of HOP in plants. In addition, we discuss the recent breakthroughs in the field and the possible new avenues for the study of plant HOP proteins in the future. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-10 |
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/11336/211435 Toribio, René; Mangano, Silvina; Fernández Bautista, Nuria; Muñoz, Alfonso; Castellano, M. Mar; HOP, a Co-chaperone Involved in Response to Stress in Plants; Frontiers Media; Frontiers in Plant Science; 11; 10-2020; 1-8 1664-462X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/211435 |
identifier_str_mv |
Toribio, René; Mangano, Silvina; Fernández Bautista, Nuria; Muñoz, Alfonso; Castellano, M. Mar; HOP, a Co-chaperone Involved in Response to Stress in Plants; Frontiers Media; Frontiers in Plant Science; 11; 10-2020; 1-8 1664-462X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2020.591940 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Frontiers Media |
publisher.none.fl_str_mv |
Frontiers Media |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.13397 |