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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/151781
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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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1844613960493432832 |
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13.070432 |