Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling

Autores
Iglesias, María José; Terrile, Maria Cecilia; Correa Aragunde, Maria Natalia; Colman, Silvana Lorena; Izquierdo Álvarez, Alicia; Fiol, Diego Fernando; Paris, Ramiro; Sánchez López, Nuria; Marina, Anabel; Calderón Villalobos, Luz Irina A.; Estelle, Mark; Lamattina, Lorenzo; Martínez Ruiz, Antonio; Casalongué, Claudia Anahí
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The F-box proteins (FBPs) TIR1/AFBs are the substrate recognition subunits of SKP1–cullin–F-box (SCF) ubiquitin ligase complexes and together with Aux/IAAs form the auxin co-receptor. Although tremendous knowledge on auxin perception and signaling has been gained in the last years, SCFTIR1/AFBs complex assembly and stabilization are emerging as new layers of regulation. Here, we investigated how nitric oxide (NO), through S-nitrosylation of ASK1 is involved in SCFTIR1/AFBs assembly. We demonstrate that ASK1 is S-nitrosylated and S-glutathionylated in cysteine (Cys) 37 and Cys118 residues in vitro. Both, in vitro and in vivo protein-protein interaction assays show that NO enhances ASK1 binding to CUL1 and TIR1/AFB2, required for SCFTIR1/AFB2 assembly. In addition, we demonstrate that Cys37 and Cys118 are essential residues for proper activation of auxin signaling pathway in planta. Phylogenetic analysis revealed that Cys37 residue is only conserved in SKP proteins in Angiosperms, suggesting that S-nitrosylation on Cys37 could represent an evolutionary adaption for SKP1 function in flowering plants. Collectively, these findings indicate that multiple events of redox modifications might be part of a fine-tuning regulation of SCFTIR1/AFBs for proper auxin signal transduction.
Fil: Iglesias, María José. Universidad Nacional de Mar del Plata; Argentina
Fil: Terrile, Maria Cecilia. Universidad Nacional de Mar del Plata; Argentina
Fil: Correa Aragunde, Maria Natalia. Universidad Nacional de Mar del Plata; Argentina
Fil: Colman, Silvana Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Izquierdo Álvarez, Alicia. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España
Fil: Fiol, Diego Fernando. Universidad Nacional de Mar del Plata; Argentina
Fil: Paris, Ramiro. Universidad Nacional de Mar del Plata; Argentina
Fil: Sánchez López, Nuria. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Marina, Anabel. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Calderón Villalobos, Luz Irina A.. Leibniz Institut Fur Pflanzenbiochemie;
Fil: Estelle, Mark. Section Of Cell And Developmental Biology; . University of California at San Diego; Estados Unidos
Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Martínez Ruiz, Antonio. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España
Fil: Casalongué, Claudia Anahí. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Materia
Arabidopsis thaliana
Ask1
Auxin signaling
Nitric Oxide
SCF E3 ligase complex
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:11336/88129
Acceder
id CONICETDig_cc76efa013597b128606dc982a4ddc70
oai_identifier_str oai:ri.conicet.gov.ar:11336/88129
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signalingIglesias, María JoséTerrile, Maria CeciliaCorrea Aragunde, Maria NataliaColman, Silvana LorenaIzquierdo Álvarez, AliciaFiol, Diego FernandoParis, RamiroSánchez López, NuriaMarina, AnabelCalderón Villalobos, Luz Irina A.Estelle, MarkLamattina, LorenzoMartínez Ruiz, AntonioCasalongué, Claudia AnahíArabidopsis thalianaAsk1Auxin signalingNitric OxideSCF E3 ligase complexhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The F-box proteins (FBPs) TIR1/AFBs are the substrate recognition subunits of SKP1–cullin–F-box (SCF) ubiquitin ligase complexes and together with Aux/IAAs form the auxin co-receptor. Although tremendous knowledge on auxin perception and signaling has been gained in the last years, SCFTIR1/AFBs complex assembly and stabilization are emerging as new layers of regulation. Here, we investigated how nitric oxide (NO), through S-nitrosylation of ASK1 is involved in SCFTIR1/AFBs assembly. We demonstrate that ASK1 is S-nitrosylated and S-glutathionylated in cysteine (Cys) 37 and Cys118 residues in vitro. Both, in vitro and in vivo protein-protein interaction assays show that NO enhances ASK1 binding to CUL1 and TIR1/AFB2, required for SCFTIR1/AFB2 assembly. In addition, we demonstrate that Cys37 and Cys118 are essential residues for proper activation of auxin signaling pathway in planta. Phylogenetic analysis revealed that Cys37 residue is only conserved in SKP proteins in Angiosperms, suggesting that S-nitrosylation on Cys37 could represent an evolutionary adaption for SKP1 function in flowering plants. Collectively, these findings indicate that multiple events of redox modifications might be part of a fine-tuning regulation of SCFTIR1/AFBs for proper auxin signal transduction.Fil: Iglesias, María José. Universidad Nacional de Mar del Plata; ArgentinaFil: Terrile, Maria Cecilia. Universidad Nacional de Mar del Plata; ArgentinaFil: Correa Aragunde, Maria Natalia. Universidad Nacional de Mar del Plata; ArgentinaFil: Colman, Silvana Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Izquierdo Álvarez, Alicia. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; EspañaFil: Fiol, Diego Fernando. Universidad Nacional de Mar del Plata; ArgentinaFil: Paris, Ramiro. Universidad Nacional de Mar del Plata; ArgentinaFil: Sánchez López, Nuria. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;Fil: Marina, Anabel. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;Fil: Calderón Villalobos, Luz Irina A.. Leibniz Institut Fur Pflanzenbiochemie;Fil: Estelle, Mark. Section Of Cell And Developmental Biology; . University of California at San Diego; Estados UnidosFil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Martínez Ruiz, Antonio. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; EspañaFil: Casalongué, Claudia Anahí. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaElsevier2018-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/88129Iglesias, María José; Terrile, Maria Cecilia; Correa Aragunde, Maria Natalia; Colman, Silvana Lorena; Izquierdo Álvarez, Alicia; et al.; Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling; Elsevier; Redox Biology; 18; 9-2018; 200-2102213-2317CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.redox.2018.07.003info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2213231718304142?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:49:46Zoai:ri.conicet.gov.ar:11336/88129instacron: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 09:49:46.81CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
title Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
spellingShingle Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
Iglesias, María José
Arabidopsis thaliana
Ask1
Auxin signaling
Nitric Oxide
SCF E3 ligase complex
title_short Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
title_full Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
title_fullStr Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
title_full_unstemmed Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
title_sort Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling
dc.creator.none.fl_str_mv Iglesias, María José
Terrile, Maria Cecilia
Correa Aragunde, Maria Natalia
Colman, Silvana Lorena
Izquierdo Álvarez, Alicia
Fiol, Diego Fernando
Paris, Ramiro
Sánchez López, Nuria
Marina, Anabel
Calderón Villalobos, Luz Irina A.
Estelle, Mark
Lamattina, Lorenzo
Martínez Ruiz, Antonio
Casalongué, Claudia Anahí
author Iglesias, María José
author_facet Iglesias, María José
Terrile, Maria Cecilia
Correa Aragunde, Maria Natalia
Colman, Silvana Lorena
Izquierdo Álvarez, Alicia
Fiol, Diego Fernando
Paris, Ramiro
Sánchez López, Nuria
Marina, Anabel
Calderón Villalobos, Luz Irina A.
Estelle, Mark
Lamattina, Lorenzo
Martínez Ruiz, Antonio
Casalongué, Claudia Anahí
author_role author
author2 Terrile, Maria Cecilia
Correa Aragunde, Maria Natalia
Colman, Silvana Lorena
Izquierdo Álvarez, Alicia
Fiol, Diego Fernando
Paris, Ramiro
Sánchez López, Nuria
Marina, Anabel
Calderón Villalobos, Luz Irina A.
Estelle, Mark
Lamattina, Lorenzo
Martínez Ruiz, Antonio
Casalongué, Claudia Anahí
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Arabidopsis thaliana
Ask1
Auxin signaling
Nitric Oxide
SCF E3 ligase complex
topic Arabidopsis thaliana
Ask1
Auxin signaling
Nitric Oxide
SCF E3 ligase complex
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The F-box proteins (FBPs) TIR1/AFBs are the substrate recognition subunits of SKP1–cullin–F-box (SCF) ubiquitin ligase complexes and together with Aux/IAAs form the auxin co-receptor. Although tremendous knowledge on auxin perception and signaling has been gained in the last years, SCFTIR1/AFBs complex assembly and stabilization are emerging as new layers of regulation. Here, we investigated how nitric oxide (NO), through S-nitrosylation of ASK1 is involved in SCFTIR1/AFBs assembly. We demonstrate that ASK1 is S-nitrosylated and S-glutathionylated in cysteine (Cys) 37 and Cys118 residues in vitro. Both, in vitro and in vivo protein-protein interaction assays show that NO enhances ASK1 binding to CUL1 and TIR1/AFB2, required for SCFTIR1/AFB2 assembly. In addition, we demonstrate that Cys37 and Cys118 are essential residues for proper activation of auxin signaling pathway in planta. Phylogenetic analysis revealed that Cys37 residue is only conserved in SKP proteins in Angiosperms, suggesting that S-nitrosylation on Cys37 could represent an evolutionary adaption for SKP1 function in flowering plants. Collectively, these findings indicate that multiple events of redox modifications might be part of a fine-tuning regulation of SCFTIR1/AFBs for proper auxin signal transduction.
Fil: Iglesias, María José. Universidad Nacional de Mar del Plata; Argentina
Fil: Terrile, Maria Cecilia. Universidad Nacional de Mar del Plata; Argentina
Fil: Correa Aragunde, Maria Natalia. Universidad Nacional de Mar del Plata; Argentina
Fil: Colman, Silvana Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Izquierdo Álvarez, Alicia. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España
Fil: Fiol, Diego Fernando. Universidad Nacional de Mar del Plata; Argentina
Fil: Paris, Ramiro. Universidad Nacional de Mar del Plata; Argentina
Fil: Sánchez López, Nuria. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Marina, Anabel. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Calderón Villalobos, Luz Irina A.. Leibniz Institut Fur Pflanzenbiochemie;
Fil: Estelle, Mark. Section Of Cell And Developmental Biology; . University of California at San Diego; Estados Unidos
Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Martínez Ruiz, Antonio. Universidad Autonoma de Madrid. Hospital Universitario de la Princesa; España
Fil: Casalongué, Claudia Anahí. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
description The F-box proteins (FBPs) TIR1/AFBs are the substrate recognition subunits of SKP1–cullin–F-box (SCF) ubiquitin ligase complexes and together with Aux/IAAs form the auxin co-receptor. Although tremendous knowledge on auxin perception and signaling has been gained in the last years, SCFTIR1/AFBs complex assembly and stabilization are emerging as new layers of regulation. Here, we investigated how nitric oxide (NO), through S-nitrosylation of ASK1 is involved in SCFTIR1/AFBs assembly. We demonstrate that ASK1 is S-nitrosylated and S-glutathionylated in cysteine (Cys) 37 and Cys118 residues in vitro. Both, in vitro and in vivo protein-protein interaction assays show that NO enhances ASK1 binding to CUL1 and TIR1/AFB2, required for SCFTIR1/AFB2 assembly. In addition, we demonstrate that Cys37 and Cys118 are essential residues for proper activation of auxin signaling pathway in planta. Phylogenetic analysis revealed that Cys37 residue is only conserved in SKP proteins in Angiosperms, suggesting that S-nitrosylation on Cys37 could represent an evolutionary adaption for SKP1 function in flowering plants. Collectively, these findings indicate that multiple events of redox modifications might be part of a fine-tuning regulation of SCFTIR1/AFBs for proper auxin signal transduction.
publishDate 2018
dc.date.none.fl_str_mv 2018-09
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/11336/88129
Iglesias, María José; Terrile, Maria Cecilia; Correa Aragunde, Maria Natalia; Colman, Silvana Lorena; Izquierdo Álvarez, Alicia; et al.; Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling; Elsevier; Redox Biology; 18; 9-2018; 200-210
2213-2317
CONICET Digital
CONICET
url http://hdl.handle.net/11336/88129
identifier_str_mv Iglesias, María José; Terrile, Maria Cecilia; Correa Aragunde, Maria Natalia; Colman, Silvana Lorena; Izquierdo Álvarez, Alicia; et al.; Regulation of SCFTIR1/AFBs E3 ligase assembly by S-nitrosylation of Arabidopsis SKP1-like1 impacts on auxin signaling; Elsevier; Redox Biology; 18; 9-2018; 200-210
2213-2317
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.redox.2018.07.003
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2213231718304142?via%3Dihub
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
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.13397

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