Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants

Autores
Maselli, Gustavo Ariel; Slamovits, Claudio H.; Bianchi, Javier Ignacio; Vilarrasa Blasi, Josep; Caño Delgado, Ana I.; Mora Garcia, Santiago
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein phosphatases with Kelch-like domains (PPKL) are members of the phosphoprotein phosphatases family present only in plants and alveolates. PPKL have been described as positive effectors of brassinosteroid (BR) signaling in plants. Most of the evidence supporting this role has been gathered using one of the four homologs in Arabidopsis (Arabidopsis thaliana), brassinosteroid-insensitive1 suppressor (BSU1). We reappraised the roles of the other three members of the family, BSL1, BSL2, and BSL3, through phylogenetic, functional, and genetic analyses. We show that BSL1 and BSL2/BSL3 belong to two ancient evolutionary clades that have been highly conserved in land plants. In contrast, BSU1-type genes are exclusively found in the Brassicaceae and display a remarkable sequence divergence, even among closely related species. Simultaneous loss of function of the close paralogs BSL2 and BSL3 brings about a peculiar array of phenotypic alterations, but with marginal effects on BR signaling; loss of function of BSL1 is, in turn, phenotypically silent. Still, the products of these three genes account for the bulk of PPKL-related activity in Arabidopsis and together have an essential role in the early stages of development that BSU1 is unable to supplement. Our results underline the functional relevance of BSL phosphatases in plants and suggest that BSL2/BSL3 and BSU1 may have contrasting effects on BR signaling. Given that BSU1-type genes have likely undergone a functional shift and are phylogenetically restricted, we caution that inferences based on these genes to the whole family or to other species may be misleading.
Fil: Maselli, Gustavo Ariel. 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: Slamovits, Claudio H.. Dalhousie University Halifax; Canadá
Fil: Bianchi, Javier Ignacio. 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: Vilarrasa Blasi, Josep. Consorci CSIC-IRTA-UAB; España
Fil: Caño Delgado, Ana I.. Consorci CSIC-IRTA-UAB; España
Fil: Mora Garcia, Santiago. 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
Materia
Ppkl
Brassinosteroid
Signaling
Evolution
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:11336/23133
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/23133
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plantsMaselli, Gustavo ArielSlamovits, Claudio H.Bianchi, Javier IgnacioVilarrasa Blasi, JosepCaño Delgado, Ana I.Mora Garcia, SantiagoPpklBrassinosteroidSignalingEvolutionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Protein phosphatases with Kelch-like domains (PPKL) are members of the phosphoprotein phosphatases family present only in plants and alveolates. PPKL have been described as positive effectors of brassinosteroid (BR) signaling in plants. Most of the evidence supporting this role has been gathered using one of the four homologs in Arabidopsis (Arabidopsis thaliana), brassinosteroid-insensitive1 suppressor (BSU1). We reappraised the roles of the other three members of the family, BSL1, BSL2, and BSL3, through phylogenetic, functional, and genetic analyses. We show that BSL1 and BSL2/BSL3 belong to two ancient evolutionary clades that have been highly conserved in land plants. In contrast, BSU1-type genes are exclusively found in the Brassicaceae and display a remarkable sequence divergence, even among closely related species. Simultaneous loss of function of the close paralogs BSL2 and BSL3 brings about a peculiar array of phenotypic alterations, but with marginal effects on BR signaling; loss of function of BSL1 is, in turn, phenotypically silent. Still, the products of these three genes account for the bulk of PPKL-related activity in Arabidopsis and together have an essential role in the early stages of development that BSU1 is unable to supplement. Our results underline the functional relevance of BSL phosphatases in plants and suggest that BSL2/BSL3 and BSU1 may have contrasting effects on BR signaling. Given that BSU1-type genes have likely undergone a functional shift and are phylogenetically restricted, we caution that inferences based on these genes to the whole family or to other species may be misleading.Fil: Maselli, Gustavo Ariel. 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: Slamovits, Claudio H.. Dalhousie University Halifax; CanadáFil: Bianchi, Javier Ignacio. 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: Vilarrasa Blasi, Josep. Consorci CSIC-IRTA-UAB; EspañaFil: Caño Delgado, Ana I.. Consorci CSIC-IRTA-UAB; EspañaFil: Mora Garcia, Santiago. 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; ArgentinaAmerican Society of Plant Biologist2014-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/23133Maselli, Gustavo Ariel; Slamovits, Claudio H.; Bianchi, Javier Ignacio; Vilarrasa Blasi, Josep; Caño Delgado, Ana I.; et al.; Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants; American Society of Plant Biologist; Plant Physiology; 164; 3; 3-2014; 1527-15410032-08891532-2548CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.plantphysiol.org/content/164/3/1527info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.113.233627info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:08:54Zoai:ri.conicet.gov.ar:11336/23133instacron: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 11:08:55.023CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
title Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
spellingShingle Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
Maselli, Gustavo Ariel
Ppkl
Brassinosteroid
Signaling
Evolution
title_short Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
title_full Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
title_fullStr Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
title_full_unstemmed Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
title_sort Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants
dc.creator.none.fl_str_mv Maselli, Gustavo Ariel
Slamovits, Claudio H.
Bianchi, Javier Ignacio
Vilarrasa Blasi, Josep
Caño Delgado, Ana I.
Mora Garcia, Santiago
author Maselli, Gustavo Ariel
author_facet Maselli, Gustavo Ariel
Slamovits, Claudio H.
Bianchi, Javier Ignacio
Vilarrasa Blasi, Josep
Caño Delgado, Ana I.
Mora Garcia, Santiago
author_role author
author2 Slamovits, Claudio H.
Bianchi, Javier Ignacio
Vilarrasa Blasi, Josep
Caño Delgado, Ana I.
Mora Garcia, Santiago
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ppkl
Brassinosteroid
Signaling
Evolution
topic Ppkl
Brassinosteroid
Signaling
Evolution
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 phosphatases with Kelch-like domains (PPKL) are members of the phosphoprotein phosphatases family present only in plants and alveolates. PPKL have been described as positive effectors of brassinosteroid (BR) signaling in plants. Most of the evidence supporting this role has been gathered using one of the four homologs in Arabidopsis (Arabidopsis thaliana), brassinosteroid-insensitive1 suppressor (BSU1). We reappraised the roles of the other three members of the family, BSL1, BSL2, and BSL3, through phylogenetic, functional, and genetic analyses. We show that BSL1 and BSL2/BSL3 belong to two ancient evolutionary clades that have been highly conserved in land plants. In contrast, BSU1-type genes are exclusively found in the Brassicaceae and display a remarkable sequence divergence, even among closely related species. Simultaneous loss of function of the close paralogs BSL2 and BSL3 brings about a peculiar array of phenotypic alterations, but with marginal effects on BR signaling; loss of function of BSL1 is, in turn, phenotypically silent. Still, the products of these three genes account for the bulk of PPKL-related activity in Arabidopsis and together have an essential role in the early stages of development that BSU1 is unable to supplement. Our results underline the functional relevance of BSL phosphatases in plants and suggest that BSL2/BSL3 and BSU1 may have contrasting effects on BR signaling. Given that BSU1-type genes have likely undergone a functional shift and are phylogenetically restricted, we caution that inferences based on these genes to the whole family or to other species may be misleading.
Fil: Maselli, Gustavo Ariel. 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: Slamovits, Claudio H.. Dalhousie University Halifax; Canadá
Fil: Bianchi, Javier Ignacio. 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: Vilarrasa Blasi, Josep. Consorci CSIC-IRTA-UAB; España
Fil: Caño Delgado, Ana I.. Consorci CSIC-IRTA-UAB; España
Fil: Mora Garcia, Santiago. 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
description Protein phosphatases with Kelch-like domains (PPKL) are members of the phosphoprotein phosphatases family present only in plants and alveolates. PPKL have been described as positive effectors of brassinosteroid (BR) signaling in plants. Most of the evidence supporting this role has been gathered using one of the four homologs in Arabidopsis (Arabidopsis thaliana), brassinosteroid-insensitive1 suppressor (BSU1). We reappraised the roles of the other three members of the family, BSL1, BSL2, and BSL3, through phylogenetic, functional, and genetic analyses. We show that BSL1 and BSL2/BSL3 belong to two ancient evolutionary clades that have been highly conserved in land plants. In contrast, BSU1-type genes are exclusively found in the Brassicaceae and display a remarkable sequence divergence, even among closely related species. Simultaneous loss of function of the close paralogs BSL2 and BSL3 brings about a peculiar array of phenotypic alterations, but with marginal effects on BR signaling; loss of function of BSL1 is, in turn, phenotypically silent. Still, the products of these three genes account for the bulk of PPKL-related activity in Arabidopsis and together have an essential role in the early stages of development that BSU1 is unable to supplement. Our results underline the functional relevance of BSL phosphatases in plants and suggest that BSL2/BSL3 and BSU1 may have contrasting effects on BR signaling. Given that BSU1-type genes have likely undergone a functional shift and are phylogenetically restricted, we caution that inferences based on these genes to the whole family or to other species may be misleading.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
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/11336/23133
Maselli, Gustavo Ariel; Slamovits, Claudio H.; Bianchi, Javier Ignacio; Vilarrasa Blasi, Josep; Caño Delgado, Ana I.; et al.; Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants; American Society of Plant Biologist; Plant Physiology; 164; 3; 3-2014; 1527-1541
0032-0889
1532-2548
CONICET Digital
CONICET
url http://hdl.handle.net/11336/23133
identifier_str_mv Maselli, Gustavo Ariel; Slamovits, Claudio H.; Bianchi, Javier Ignacio; Vilarrasa Blasi, Josep; Caño Delgado, Ana I.; et al.; Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants; American Society of Plant Biologist; Plant Physiology; 164; 3; 3-2014; 1527-1541
0032-0889
1532-2548
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://www.plantphysiol.org/content/164/3/1527
info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.113.233627
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society of Plant Biologist
publisher.none.fl_str_mv American Society of Plant Biologist
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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score 12.982451

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