ArticleThe Journal of biological chemistry2012
Photosensitivity of kinase activation by blue light involves the lifetime of a cysteinyl-flavin adduct intermediate, S390, in the photoreaction cycle of the LOV2 domain in phototropin, a plant blue light receptor.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Phototropin2 LOV1 plays a role in strong light signal transduction leading to chloroplast avoidance response.Acta physiologiae plantarum · 2026Article
- Genetic architecture of a light-temperature coincidence detector.Nature communications · 2025Article
- Phototropin 2 mediates daily cold priming to promote light responses in Arabidopsis.Journal of experimental botany · 2025Article
- Light quality as a driver of photosynthetic apparatus development.Biophysical reviews · 2022Review
- Moving around in a phototropic response: the phosphorylation of NPH3.Plant physiology · 2021Article
- Phosphorylation of NONPHOTOTROPIC HYPOCOTYL3 affects photosensory adaptation during the phototropic response.Plant physiology · 2021Article
- Domain Organization in Plant Blue-Light Receptor Phototropin2 ofInternational journal of molecular sciences · 2020Review
- Arabidopsis ROOT PHOTOTROPISM2 Is a Light-Dependent Dynamic Modulator of Phototropin1.The Plant cell · 2020Article
- The cold-induced switch in direction of chloroplast relocation occurs independently of changes in endogenous phototropin levels.PloS one · 2020Article
- Engineering the phototropin photocycle improves photoreceptor performance and plant biomass production.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Blue light-excited LOV1 and LOV2 domains cooperatively regulate the kinase activity of full-length phototropin2 fromThe Journal of biological chemistry · 2018Article
- Phototropin perceives temperature based on the lifetime of its photoactivated state.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Blue Light-excited Light-Oxygen-Voltage-sensing Domain 2 (LOV2) Triggers a Rearrangement of the Kinase Domain to Induce Phosphorylation Activity in Arabidopsis Phototropin1.The Journal of biological chemistry · 2016Article
- A Native Threonine Coordinates Ordered Water to Tune Light-Oxygen-Voltage (LOV) Domain Photocycle Kinetics and Osmotic Stress Signaling in Trichoderma reesei ENVOY.The Journal of biological chemistry · 2016Article
- Molecular mechanism of phototropin light signaling.Journal of plant research · 2016Review
- Arabidopsis phot1 and phot2 phosphorylate BLUS1 kinase with different efficiencies in stomatal opening.Journal of plant research · 2016Article
- Signal transduction in light-oxygen-voltage receptors lacking the adduct-forming cysteine residue.Nature communications · 2015Article
- LOV-based optogenetic devices: light-driven modules to impart photoregulated control of cellular signaling.Frontiers in molecular biosciences · 2015Review
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phototropin (phot) is a light-regulated protein kinase that mediates a variety of photoresponses in plants, such as phototropism, chloroplast positioning, and stomata opening. Arabidopsis has two homologues, phot1 and phot2, that share physiological functions depending on light intensity. A phot molecule has two photoreceptive light oxygen voltage-sensing domains, LOV1 and LOV2, and a Ser/Thr kinase domain. The LOV domains undergo a photocycle upon blue light (BL) stimulation, including transient adduct formation between the chromophore and a conserved cysteine (S390 intermediate) that leads to activation of the kinase. To uncover the mechanism underlying the photoactivation of the kinase, we have introduced a kinase assay system composed of a phot1 LOV2-linker-kinase polypeptide as a light-regulated kinase and its N-terminal polypeptide as an artificial substrate (Okajima, K., Matsuoka, D., and Tokutomi, S. (2011) LOV2-linker-kinase phosphorylates LOV1-containing N-terminal polypeptide substrate via photoreaction of LOV2 in Arabidopsis phototropin1. FEBS Lett. 585, 3391-3395). In the present study, we extended the assay system to phot2 and compared the photochemistry and kinase activation by BL between phot1 and phot2 to gain insight into the molecular basis for the different photosensitivities of phot1 and phot2. Photosensitivity of kinase activation by BL and the lifetime of S390 of phot1 were 10 times higher and longer, respectively, than those of phot2. This correlation was confirmed by an amino acid substitution experiment with phot1 to shorten the lifetime of S390. The present results demonstrated that the photosensitivity of kinase activation in phot involves the lifetime of S390 in LOV2, suggesting that the lifetime is one of the key factors for the different photosensitivities observed for phot1 and phot2.
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