Phosphorylation of Arabidopsis UVR8 photoreceptor modulates protein interactions and responses to UV-B radiation

Wei Liu, Giovanni Giuriani, Anezka Havlikova, Dezhi Li, Douglas J. Lamont, Susanne Neugart, Christos N. Velanis, Jan Petersen, Ute Hoecker, John M. Christie and Gareth I. Jenkins ()
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Wei Liu: University of Glasgow
Giovanni Giuriani: University of Glasgow
Anezka Havlikova: University of Glasgow
Dezhi Li: University of Glasgow
Douglas J. Lamont: University of Dundee
Susanne Neugart: Georg-August-Universität Göttingen
Christos N. Velanis: University of Glasgow
Jan Petersen: University of Glasgow
Ute Hoecker: University of Köln
John M. Christie: University of Glasgow
Gareth I. Jenkins: University of Glasgow

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Exposure of plants to ultraviolet-B (UV-B) radiation initiates transcriptional responses that modify metabolism, physiology and development to enhance viability in sunlight. Many of these regulatory responses to UV-B radiation are mediated by the photoreceptor UV RESISTANCE LOCUS 8 (UVR8). Following photoreception, UVR8 interacts directly with multiple proteins to regulate gene expression, but the mechanisms that control differential protein binding to initiate distinct responses are unknown. Here we show that UVR8 is phosphorylated at several sites and that UV-B stimulates phosphorylation at Serine 402. Site-directed mutagenesis to mimic Serine 402 phosphorylation promotes binding of UVR8 to REPRESSOR OF UV-B PHOTOMORPHOGENESIS (RUP) proteins, which negatively regulate UVR8 action. Complementation of the uvr8 mutant with phosphonull or phosphomimetic variants suggests that phosphorylation of Serine 402 modifies UVR8 activity and promotes flavonoid biosynthesis, a key UV-B-stimulated response that enhances plant protection and crop nutritional quality. This research provides a basis to understand how UVR8 interacts differentially with effector proteins to regulate plant responses to UV-B radiation.

Date: 2024
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DOI: 10.1038/s41467-024-45575-7

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