Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling

Autores
Viczián, András; Ádám, Éva; Staudt, Anne Marie; Lambert, Dorothee; Klement, Eva; Romero Montepaone, Sofía Iara; Hiltbrunner, Andreas; Casal, Jorge José; Schäfer, Eberhard; Nagy, Ferenc; Klose, Cornelia
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Phytochrome B (phyB) is an excellent light quality and quantity sensor that can detect subtle changes in the light environment. The relative amounts of the biologically active photoreceptor (phyB Pfr) are determined by the light conditions and light independent thermal relaxation of Pfr into the inactive phyB Pr, termed thermal reversion. Little is known about the regulation of thermal reversion and how it affects plants’ light sensitivity. In this study we identified several serine/threonine residues on the N-terminal extension (NTE) of Arabidopsis thaliana phyB that are differentially phosphorylated in response to light and temperature, and examined transgenic plants expressing nonphosphorylatable and phosphomimic phyB mutants. The NTE of phyB is essential for thermal stability of the Pfr form, and phosphorylation of S86 particularly enhances the thermal reversion rate of the phyB Pfr–Pr heterodimer in vivo. We demonstrate that S86 phosphorylation is especially critical for phyB signaling compared with phosphorylation of the more N-terminal residues. Interestingly, S86 phosphorylation is reduced in light, paralleled by a progressive Pfr stabilization under prolonged irradiation. By investigating other phytochromes (phyD and phyE) we provide evidence that acceleration of thermal reversion by phosphorylation represents a general mechanism for attenuating phytochrome signaling.
Fil: Viczián, András. Institute of Plant Biology; Hungría
Fil: Ádám, Éva. Institute of Plant Biology; Hungría. University of Szeged; Hungría
Fil: Staudt, Anne Marie. Albert Ludwigs University of Freiburg; Alemania
Fil: Lambert, Dorothee. Albert Ludwigs University of Freiburg; Alemania
Fil: Klement, Eva. Biological Research Centre; Hungría
Fil: Romero Montepaone, Sofía Iara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura; Argentina
Fil: Hiltbrunner, Andreas. Albert Ludwigs University of Freiburg; Alemania
Fil: Casal, Jorge José. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura; Argentina. 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: Schäfer, Eberhard. Albert Ludwigs University of Freiburg; Alemania
Fil: Nagy, Ferenc. Institute of Plant Biology; Hungría
Fil: Klose, Cornelia. Albert Ludwigs University of Freiburg; Alemania
Materia
DARK REVERSION
PHOSPHORYLATION
PHYB NTE
PHYTOCHROME
THERMAL REVERSION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/151781

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oai_identifier_str oai:ri.conicet.gov.ar:11336/151781
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Differential phosphorylation of the N‐terminal extension regulates phytochrome B signalingViczián, AndrásÁdám, ÉvaStaudt, Anne MarieLambert, DorotheeKlement, EvaRomero Montepaone, Sofía IaraHiltbrunner, AndreasCasal, Jorge JoséSchäfer, EberhardNagy, FerencKlose, CorneliaDARK REVERSIONPHOSPHORYLATIONPHYB NTEPHYTOCHROMETHERMAL REVERSIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Phytochrome B (phyB) is an excellent light quality and quantity sensor that can detect subtle changes in the light environment. The relative amounts of the biologically active photoreceptor (phyB Pfr) are determined by the light conditions and light independent thermal relaxation of Pfr into the inactive phyB Pr, termed thermal reversion. Little is known about the regulation of thermal reversion and how it affects plants’ light sensitivity. In this study we identified several serine/threonine residues on the N-terminal extension (NTE) of Arabidopsis thaliana phyB that are differentially phosphorylated in response to light and temperature, and examined transgenic plants expressing nonphosphorylatable and phosphomimic phyB mutants. The NTE of phyB is essential for thermal stability of the Pfr form, and phosphorylation of S86 particularly enhances the thermal reversion rate of the phyB Pfr–Pr heterodimer in vivo. We demonstrate that S86 phosphorylation is especially critical for phyB signaling compared with phosphorylation of the more N-terminal residues. Interestingly, S86 phosphorylation is reduced in light, paralleled by a progressive Pfr stabilization under prolonged irradiation. By investigating other phytochromes (phyD and phyE) we provide evidence that acceleration of thermal reversion by phosphorylation represents a general mechanism for attenuating phytochrome signaling.Fil: Viczián, András. Institute of Plant Biology; HungríaFil: Ádám, Éva. Institute of Plant Biology; Hungría. University of Szeged; HungríaFil: Staudt, Anne Marie. Albert Ludwigs University of Freiburg; AlemaniaFil: Lambert, Dorothee. Albert Ludwigs University of Freiburg; AlemaniaFil: Klement, Eva. Biological Research Centre; HungríaFil: Romero Montepaone, Sofía Iara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura; ArgentinaFil: Hiltbrunner, Andreas. Albert Ludwigs University of Freiburg; AlemaniaFil: Casal, Jorge José. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura; Argentina. 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: Schäfer, Eberhard. Albert Ludwigs University of Freiburg; AlemaniaFil: Nagy, Ferenc. Institute of Plant Biology; HungríaFil: Klose, Cornelia. Albert Ludwigs University of Freiburg; AlemaniaWiley Blackwell Publishing, Inc2019-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/151781Viczián, András; Ádám, Éva; Staudt, Anne Marie; Lambert, Dorothee; Klement, Eva; et al.; Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling; Wiley Blackwell Publishing, Inc; New Phytologist; 225; 4; 11-2019; 1635-16500028-646XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/nph.16243info:eu-repo/semantics/altIdentifier/doi/10.1111/nph.16243info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:08:52Zoai:ri.conicet.gov.ar:11336/151781instacron: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:34982025-09-29 10:08:52.939CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
title Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
spellingShingle Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
Viczián, András
DARK REVERSION
PHOSPHORYLATION
PHYB NTE
PHYTOCHROME
THERMAL REVERSION
title_short Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
title_full Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
title_fullStr Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
title_full_unstemmed Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
title_sort Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling
dc.creator.none.fl_str_mv Viczián, András
Ádám, Éva
Staudt, Anne Marie
Lambert, Dorothee
Klement, Eva
Romero Montepaone, Sofía Iara
Hiltbrunner, Andreas
Casal, Jorge José
Schäfer, Eberhard
Nagy, Ferenc
Klose, Cornelia
author Viczián, András
author_facet Viczián, András
Ádám, Éva
Staudt, Anne Marie
Lambert, Dorothee
Klement, Eva
Romero Montepaone, Sofía Iara
Hiltbrunner, Andreas
Casal, Jorge José
Schäfer, Eberhard
Nagy, Ferenc
Klose, Cornelia
author_role author
author2 Ádám, Éva
Staudt, Anne Marie
Lambert, Dorothee
Klement, Eva
Romero Montepaone, Sofía Iara
Hiltbrunner, Andreas
Casal, Jorge José
Schäfer, Eberhard
Nagy, Ferenc
Klose, Cornelia
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv DARK REVERSION
PHOSPHORYLATION
PHYB NTE
PHYTOCHROME
THERMAL REVERSION
topic DARK REVERSION
PHOSPHORYLATION
PHYB NTE
PHYTOCHROME
THERMAL REVERSION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Phytochrome B (phyB) is an excellent light quality and quantity sensor that can detect subtle changes in the light environment. The relative amounts of the biologically active photoreceptor (phyB Pfr) are determined by the light conditions and light independent thermal relaxation of Pfr into the inactive phyB Pr, termed thermal reversion. Little is known about the regulation of thermal reversion and how it affects plants’ light sensitivity. In this study we identified several serine/threonine residues on the N-terminal extension (NTE) of Arabidopsis thaliana phyB that are differentially phosphorylated in response to light and temperature, and examined transgenic plants expressing nonphosphorylatable and phosphomimic phyB mutants. The NTE of phyB is essential for thermal stability of the Pfr form, and phosphorylation of S86 particularly enhances the thermal reversion rate of the phyB Pfr–Pr heterodimer in vivo. We demonstrate that S86 phosphorylation is especially critical for phyB signaling compared with phosphorylation of the more N-terminal residues. Interestingly, S86 phosphorylation is reduced in light, paralleled by a progressive Pfr stabilization under prolonged irradiation. By investigating other phytochromes (phyD and phyE) we provide evidence that acceleration of thermal reversion by phosphorylation represents a general mechanism for attenuating phytochrome signaling.
Fil: Viczián, András. Institute of Plant Biology; Hungría
Fil: Ádám, Éva. Institute of Plant Biology; Hungría. University of Szeged; Hungría
Fil: Staudt, Anne Marie. Albert Ludwigs University of Freiburg; Alemania
Fil: Lambert, Dorothee. Albert Ludwigs University of Freiburg; Alemania
Fil: Klement, Eva. Biological Research Centre; Hungría
Fil: Romero Montepaone, Sofía Iara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura; Argentina
Fil: Hiltbrunner, Andreas. Albert Ludwigs University of Freiburg; Alemania
Fil: Casal, Jorge José. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones Fisiológicas y Ecológicas Vinculadas a la Agricultura; Argentina. 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: Schäfer, Eberhard. Albert Ludwigs University of Freiburg; Alemania
Fil: Nagy, Ferenc. Institute of Plant Biology; Hungría
Fil: Klose, Cornelia. Albert Ludwigs University of Freiburg; Alemania
description Phytochrome B (phyB) is an excellent light quality and quantity sensor that can detect subtle changes in the light environment. The relative amounts of the biologically active photoreceptor (phyB Pfr) are determined by the light conditions and light independent thermal relaxation of Pfr into the inactive phyB Pr, termed thermal reversion. Little is known about the regulation of thermal reversion and how it affects plants’ light sensitivity. In this study we identified several serine/threonine residues on the N-terminal extension (NTE) of Arabidopsis thaliana phyB that are differentially phosphorylated in response to light and temperature, and examined transgenic plants expressing nonphosphorylatable and phosphomimic phyB mutants. The NTE of phyB is essential for thermal stability of the Pfr form, and phosphorylation of S86 particularly enhances the thermal reversion rate of the phyB Pfr–Pr heterodimer in vivo. We demonstrate that S86 phosphorylation is especially critical for phyB signaling compared with phosphorylation of the more N-terminal residues. Interestingly, S86 phosphorylation is reduced in light, paralleled by a progressive Pfr stabilization under prolonged irradiation. By investigating other phytochromes (phyD and phyE) we provide evidence that acceleration of thermal reversion by phosphorylation represents a general mechanism for attenuating phytochrome signaling.
publishDate 2019
dc.date.none.fl_str_mv 2019-11
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/11336/151781
Viczián, András; Ádám, Éva; Staudt, Anne Marie; Lambert, Dorothee; Klement, Eva; et al.; Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling; Wiley Blackwell Publishing, Inc; New Phytologist; 225; 4; 11-2019; 1635-1650
0028-646X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/151781
identifier_str_mv Viczián, András; Ádám, Éva; Staudt, Anne Marie; Lambert, Dorothee; Klement, Eva; et al.; Differential phosphorylation of the N‐terminal extension regulates phytochrome B signaling; Wiley Blackwell Publishing, Inc; New Phytologist; 225; 4; 11-2019; 1635-1650
0028-646X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/nph.16243
info:eu-repo/semantics/altIdentifier/doi/10.1111/nph.16243
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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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