Phosphorylation of Phytochrome B Inhibits Light-Induced Signaling via Accelerated Dark Reversion in Arabidopsis.

Détails

ID Serval
serval:BIB_3FAB7C6FEE21
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Phosphorylation of Phytochrome B Inhibits Light-Induced Signaling via Accelerated Dark Reversion in Arabidopsis.
Périodique
Plant Cell
Auteur(s)
Medzihradszky M., Bindics J., Adám E., Viczián A., Klement E., Lorrain S., Gyula P., Mérai Z., Fankhauser C., Medzihradszky K.F., Kunkel T., Schäfer E., Nagy F.
ISSN
1532-298X (Electronic)
ISSN-L
1040-4651
Statut éditorial
Publié
Date de publication
2013
Volume
25
Numéro
2
Pages
535-544
Langue
anglais
Résumé
The photoreceptor phytochrome B (phyB) interconverts between the biologically active Pfr (λmax = 730 nm) and inactive Pr (λmax = 660 nm) forms in a red/far-red-dependent fashion and regulates, as molecular switch, many aspects of light-dependent development in Arabidopsis thaliana. phyB signaling is launched by the biologically active Pfr conformer and mediated by specific protein-protein interactions between phyB Pfr and its downstream regulatory partners, whereas conversion of Pfr to Pr terminates signaling. Here, we provide evidence that phyB is phosphorylated in planta at Ser-86 located in the N-terminal domain of the photoreceptor. Analysis of phyB-9 transgenic plants expressing phospho-mimic and nonphosphorylatable phyB-yellow fluorescent protein (YFP) fusions demonstrated that phosphorylation of Ser-86 negatively regulates all physiological responses tested. The Ser86Asp and Ser86Ala substitutions do not affect stability, photoconversion, and spectral properties of the photoreceptor, but light-independent relaxation of the phyB(Ser86Asp) Pfr into Pr, also termed dark reversion, is strongly enhanced both in vivo and in vitro. Faster dark reversion attenuates red light-induced nuclear import and interaction of phyB(Ser86Asp)-YFP Pfr with the negative regulator PHYTOCHROME INTERACTING FACTOR3 compared with phyB-green fluorescent protein. These data suggest that accelerated inactivation of the photoreceptor phyB via phosphorylation of Ser-86 represents a new paradigm for modulating phytochrome-controlled signaling.
Pubmed
Web of science
Open Access
Oui
Création de la notice
03/05/2013 9:38
Dernière modification de la notice
20/08/2019 14:36
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