ArticleThe Plant cell2009
Phytochrome A mediates rapid red light-induced phosphorylation of Arabidopsis FAR-RED ELONGATED HYPOCOTYL1 in a low fluence response.
Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Liquid-liquid phase separation of TZP promotes PPK-mediated phosphorylation of the phytochrome A photoreceptor.Nature plants · 2024Article
- Application of Multi-Omics Technologies to the Study of Phytochromes in Plants.Antioxidants (Basel, Switzerland) · 2024Review
- Phytochrome phosphorylation in plant light signaling.Frontiers in plant science · 2024Review
- Two Distinct Molecular Types of Phytochrome A in Plants: Evidence of Existence and Implications for Functioning.International journal of molecular sciences · 2023Review
- Regulation of Plant Photoresponses by Protein Kinase Activity of Phytochrome A.International journal of molecular sciences · 2023Review
- Article
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- Genome-wide association studies for soybean epicotyl length in two environments using 3VmrMLM.Frontiers in plant science · 2022Article
- Phytochrome Signaling Networks.Annual review of plant biology · 2021Review
- A LexA-based yeast two-hybrid system for studying light-switchable interactions of phytochromes with their interacting partners.aBIOTECH · 2021Article
- Article
- Molecular mechanisms underlying phytochrome-controlled morphogenesis in plants.Nature communications · 2019Review
- Plant Phytochromes and their Phosphorylation.International journal of molecular sciences · 2019Review
- Hinge region ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Direct Control of SPEECHLESS by PIF4 in the High-Temperature Response of Stomatal Development.Current biology : CB · 2018Article
- TANDEM ZINC-FINGER/PLUS3 Is a Key Component of Phytochrome A Signaling.The Plant cell · 2018Article
- Evidence that phytochrome functions as a protein kinase in plant light signalling.Nature communications · 2016Article
- Large-scale comparative phosphoprotein analysis of maize seedling leaves during greening.Planta · 2016Article
- Molecular mechanisms for mediating light-dependent nucleo/cytoplasmic partitioning of phytochrome photoreceptors.The New phytologist · 2015Review
- Photoreceptor partner FHY1 has an independent role in gene modulation and plant development under far-red light.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Phytochrome A (phyA) is the primary photoreceptor for mediating the far-red high irradiance response in Arabidopsis thaliana. FAR-RED ELONGATED HYPOCOTYL1 (FHY1) and its homolog FHY1-LIKE (FHL) define two positive regulators in the phyA signaling pathway. These two proteins have been reported to be essential for light-regulated phyA nuclear accumulation through direct physical interaction with phyA. Here, we report that FHY1 protein is phosphorylated rapidly after exposure to red light. Subsequent exposure to far-red light after the red light pulse reverses FHY1 phosphorylation. Such a phenomenon represents a classical red/far-red reversible low fluence response. The phosphorylation of FHY1 depends on functioning phyA but not on other phytochromes and cryptochromes. Furthermore, we demonstrate that FHY1 and FHL directly interact with phyA by bimolecular fluorescence complementation and that both FHY1 and FHL interact more stably with the Pr form of phyA in Arabidopsis seedlings by coimmunoprecipitation. Finally, in vitro kinase assays confirmed that a recombinant phyA is able to robustly phosphorylate FHY1. Together, our results suggest that phyA may differentially regulate FHY1 and FHL activity through direct physical interaction and red/far-red light reversible phosphorylation to fine-tune their degradation rates and resulting light responses.
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