ArticleThe Journal of biological chemistry2014
Light-induced conformational changes of LOV1 (light oxygen voltage-sensing domain 1) and LOV2 relative to the kinase domain and regulation of kinase activity in Chlamydomonas phototropin.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Synthetic Biology Meets CaCells · 2024Review
- Deciphering Molecular Mechanisms and Intervening in Physiological and Pathophysiological Processes of CaCells · 2021Review
- Domain Organization in Plant Blue-Light Receptor Phototropin2 ofInternational journal of molecular sciences · 2020Review
- New Light on the Mechanism of Phototransduction in Phototropin.Biochemistry · 2020Article
- Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron.IUCrJ · 2020Article
- Low-fluence blue light-induced phosphorylation of Zmphot1 mediates the first positive phototropism.Journal of experimental botany · 2019Article
- Arguments for an additional long-lived intermediate in the photocycle of the full-length aureochrome 1c receptor: A time-resolved small-angle X-ray scattering study.Structural dynamics (Melville, N.Y.) · 2019Article
- Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain ofACS omega · 2019Article
- Blue light-excited LOV1 and LOV2 domains cooperatively regulate the kinase activity of full-length phototropin2 fromThe Journal of biological chemistry · 2018Article
- Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.Scientific reports · 2017Article
- Functional characterization of a constitutively active kinase variant ofThe Journal of biological chemistry · 2017Article
- Functional characterization of Arabidopsis phototropin 1 in the hypocotyl apex.The Plant journal : for cell and molecular biology · 2016Article
- 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
- Functional and topological diversity of LOV domain photoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 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
- Editorial: Emerging Technologies for the Study of Plant Environmental Sensing.Plant & cell physiology · 2015Article
- Plant flavoprotein photoreceptors.Plant & cell physiology · 2015Review
- Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations-implications for the understanding of LOV photoactivation.Frontiers in molecular biosciences · 2015Article
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14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phototropin (phot), a blue light (BL) receptor in plants, has two photoreceptive domains named LOV1 and LOV2 as well as a Ser/Thr kinase domain (KD) and acts as a BL-regulated protein kinase. A LOV domain harbors a flavin mononucleotide that undergoes a cyclic photoreaction upon BL excitation via a signaling state in which the inhibition of the kinase activity by LOV2 is negated. To understand the molecular mechanism underlying the BL-dependent activation of the kinase, the photochemistry, kinase activity, and molecular structure were studied with the phot of Chlamydomonas reinhardtii. Full-length and LOV2-KD samples of C. reinhardtii phot showed cyclic photoreaction characteristics with the activation of LOV- and BL-dependent kinase. Truncation of LOV1 decreased the photosensitivity of the kinase activation, which was well explained by the fact that the signaling state lasted for a shorter period of time compared with that of the phot. Small angle x-ray scattering revealed monomeric forms of the proteins in solution and detected BL-dependent conformational changes, suggesting an extension of the global molecular shapes of both samples. Constructed molecular model of full-length phot based on the small angle x-ray scattering data proved the arrangement of LOV1, LOV2, and KD for the first time that showed a tandem arrangement both in the dark and under BL irradiation. The models suggest that LOV1 alters its position relative to LOV2-KD under BL irradiation. This finding demonstrates that LOV1 may interact with LOV2 and modify the photosensitivity of the kinase activation through alteration of the duration of the signaling state in LOV2.
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