Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis

Autores
Mora Garcia, Santiago; Vert, Gregory; Yin, Yanhai; Caño Delgado, Ana; Cheong, Hyeonsook; Chory, Joanne
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1. We identified bsu1-1D as a dominant suppressor of bri1 in A abidopsis. BSU1 encodes a nuclear-localized serine-threonine protein phosphatase with an N-terminal Kelch-repeat domain, and is preferentially expressed in elongating cells. BSU1 is able to modulate the phosphorylation state of BES1, counter acting the action of the glycogen synthase kinase-3 BIN2, and leading to inc eased steady-state levels of dephosphorylated BES1. BSU1 belongs to a small gene family; loss-of-function analyses unravel the extent of functional overlap among members of the family and confirm the role of these phosphatases in the control of cell elongation by BL. Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL.
Fil: Mora Garcia, Santiago. Salk Institute. Plant Biology Laboratory; Estados Unidos. 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. Howard Hughes Medical Institute; Estados Unidos
Fil: Vert, Gregory. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Yin, Yanhai. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Caño Delgado, Ana. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Cheong, Hyeonsook. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Chory, Joanne. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Materia
BRASSINOSTEROIDS
SIGNALING
PHOSPHATASE
BSL
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:11336/43668
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/43668
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in ArabidopsisMora Garcia, SantiagoVert, GregoryYin, YanhaiCaño Delgado, AnaCheong, HyeonsookChory, JoanneBRASSINOSTEROIDSSIGNALINGPHOSPHATASEBSLhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1. We identified bsu1-1D as a dominant suppressor of bri1 in A abidopsis. BSU1 encodes a nuclear-localized serine-threonine protein phosphatase with an N-terminal Kelch-repeat domain, and is preferentially expressed in elongating cells. BSU1 is able to modulate the phosphorylation state of BES1, counter acting the action of the glycogen synthase kinase-3 BIN2, and leading to inc eased steady-state levels of dephosphorylated BES1. BSU1 belongs to a small gene family; loss-of-function analyses unravel the extent of functional overlap among members of the family and confirm the role of these phosphatases in the control of cell elongation by BL. Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL.Fil: Mora Garcia, Santiago. Salk Institute. Plant Biology Laboratory; Estados Unidos. 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. Howard Hughes Medical Institute; Estados UnidosFil: Vert, Gregory. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados UnidosFil: Yin, Yanhai. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados UnidosFil: Caño Delgado, Ana. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados UnidosFil: Cheong, Hyeonsook. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados UnidosFil: Chory, Joanne. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados UnidosCold Spring Harbor Laboratory Press2004-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/43668Mora Garcia, Santiago; Vert, Gregory; Yin, Yanhai; Caño Delgado, Ana; Cheong, Hyeonsook; et al.; Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis; Cold Spring Harbor Laboratory Press; Genes & Development.; 18; 4; 2-2004; 448-4600890-93691549-5477CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://genesdev.cshlp.org/content/18/4/448.longinfo:eu-repo/semantics/altIdentifier/doi/10.1101/gad.1174204info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:28:58Zoai:ri.conicet.gov.ar:11336/43668instacron: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:34982025-10-22 11:28:58.445CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
title Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
spellingShingle Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
Mora Garcia, Santiago
BRASSINOSTEROIDS
SIGNALING
PHOSPHATASE
BSL
title_short Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
title_full Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
title_fullStr Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
title_full_unstemmed Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
title_sort Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
dc.creator.none.fl_str_mv Mora Garcia, Santiago
Vert, Gregory
Yin, Yanhai
Caño Delgado, Ana
Cheong, Hyeonsook
Chory, Joanne
author Mora Garcia, Santiago
author_facet Mora Garcia, Santiago
Vert, Gregory
Yin, Yanhai
Caño Delgado, Ana
Cheong, Hyeonsook
Chory, Joanne
author_role author
author2 Vert, Gregory
Yin, Yanhai
Caño Delgado, Ana
Cheong, Hyeonsook
Chory, Joanne
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv BRASSINOSTEROIDS
SIGNALING
PHOSPHATASE
BSL
topic BRASSINOSTEROIDS
SIGNALING
PHOSPHATASE
BSL
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1. We identified bsu1-1D as a dominant suppressor of bri1 in A abidopsis. BSU1 encodes a nuclear-localized serine-threonine protein phosphatase with an N-terminal Kelch-repeat domain, and is preferentially expressed in elongating cells. BSU1 is able to modulate the phosphorylation state of BES1, counter acting the action of the glycogen synthase kinase-3 BIN2, and leading to inc eased steady-state levels of dephosphorylated BES1. BSU1 belongs to a small gene family; loss-of-function analyses unravel the extent of functional overlap among members of the family and confirm the role of these phosphatases in the control of cell elongation by BL. Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL.
Fil: Mora Garcia, Santiago. Salk Institute. Plant Biology Laboratory; Estados Unidos. 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. Howard Hughes Medical Institute; Estados Unidos
Fil: Vert, Gregory. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Yin, Yanhai. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Caño Delgado, Ana. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Cheong, Hyeonsook. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
Fil: Chory, Joanne. Howard Hughes Medical Institute; Estados Unidos. Salk Institute. Plant Biology Laboratory; Estados Unidos
description Perception of the plant steroid hormone brassinolide (BL) by the membrane-associated receptor kinase BRI1 triggers the dephosphorylation and accumulation in the nucleus of the transcriptional modulators BES1 and BZR1. We identified bsu1-1D as a dominant suppressor of bri1 in A abidopsis. BSU1 encodes a nuclear-localized serine-threonine protein phosphatase with an N-terminal Kelch-repeat domain, and is preferentially expressed in elongating cells. BSU1 is able to modulate the phosphorylation state of BES1, counter acting the action of the glycogen synthase kinase-3 BIN2, and leading to inc eased steady-state levels of dephosphorylated BES1. BSU1 belongs to a small gene family; loss-of-function analyses unravel the extent of functional overlap among members of the family and confirm the role of these phosphatases in the control of cell elongation by BL. Our data indicate that BES1 is subject to antagonistic phosphorylation and dephosphorylation reactions in the nucleus, which fine-tune the amplitude of the response to BL.
publishDate 2004
dc.date.none.fl_str_mv 2004-02
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/11336/43668
Mora Garcia, Santiago; Vert, Gregory; Yin, Yanhai; Caño Delgado, Ana; Cheong, Hyeonsook; et al.; Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis; Cold Spring Harbor Laboratory Press; Genes & Development.; 18; 4; 2-2004; 448-460
0890-9369
1549-5477
CONICET Digital
CONICET
url http://hdl.handle.net/11336/43668
identifier_str_mv Mora Garcia, Santiago; Vert, Gregory; Yin, Yanhai; Caño Delgado, Ana; Cheong, Hyeonsook; et al.; Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis; Cold Spring Harbor Laboratory Press; Genes & Development.; 18; 4; 2-2004; 448-460
0890-9369
1549-5477
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://genesdev.cshlp.org/content/18/4/448.long
info:eu-repo/semantics/altIdentifier/doi/10.1101/gad.1174204
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 Cold Spring Harbor Laboratory Press
publisher.none.fl_str_mv Cold Spring Harbor Laboratory 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
_version_ 1846781871686418432
score 12.982451

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