Phytochrome phosphorylation modulates light signaling by influencing the protein-protein interaction

Jeong-Il Kim, Yu Shen, Yun-Jeong Han, Joung-Eun Park, Daniel Kirchenbauer, Moon-Soo Soh, Ferenc Nagy, Eberhard Schäfer, Pill-Soon Song

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Plant photoreceptor phytochromes are phosphoproteins, but the question as to the functional role of phytochrome phosphorylation has remained to be elucidated. We investigated the functional role of phytochrome phosphorylation in plant light signaling using a Pfr-specific phosphorylation site mutant, Ser598Ala of oat (Avena sativa) phytochrome A (phyA). The transgenic Arabidopsis thaliana (phyA-201 background) plants with this mutant phyA showed hypersensitivity to light, suggesting that phytochrome phosphorylation at Serine-598 (Ser598) in the hinge region is involved in an inhibitory mechanism. The phosphorylation at Ser598 prevented its interaction with putative signal transducers, Nucleoside Diphosphate Kinase-2 and Phytochrome-Interacting Factor-3. These results suggest that phosphorylation in the hinge region of phytochromes serves as a signal-modulating site through the protein-protein interaction between phytochrome and its putative signal transducer proteins.
Original languageEnglish
Pages (from-to)2629-40
Number of pages12
JournalPlant Cell
Volume16
Issue number10
DOIs
Publication statusPublished - 2004

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