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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/211435

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network_name_str CONICET Digital (CONICET)
spelling 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
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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