ArticleThe Journal of biological chemistry2018
Blue light-excited LOV1 and LOV2 domains cooperatively regulate the kinase activity of full-length phototropin2 from
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Laminar patterning transcription factors orchestrate spatial metabolite partitioning in Capsicum fruit.Nature plants · 2026Article
- Phototropin2 LOV1 plays a role in strong light signal transduction leading to chloroplast avoidance response.Acta physiologiae plantarum · 2026Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.IUCrJ · 2022Article
- Transcriptome, metabolome and suppressor analysis reveal an essential role for the ubiquitin-proteasome system in seedling chloroplast development.BMC plant biology · 2022Article
- Red light-induced structure changes in phytochrome A from Pisum sativum.Scientific reports · 2021Article
- Domain Organization in Plant Blue-Light Receptor Phototropin2 ofInternational journal of molecular sciences · 2020Review
- Low-fluence blue light-induced phosphorylation of Zmphot1 mediates the first positive phototropism.Journal of experimental botany · 2019Article
- Genetically Encoded Tools to Monitor and Interrogate Membrane Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.))Review
- Lighting the way: Recent insights into the structure and regulation of phototropin blue light receptors.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phototropin2 (phot2) is a blue-light (BL) receptor that regulates BL-dependent activities for efficient photosynthesis in plants. phot2 comprises two BL-receiving light-oxygen-voltage-sensing domains (LOV1 and LOV2) and a kinase domain. BL-excited LOV2 is thought to be primarily responsible for the BL-dependent activation of the kinase. However, the molecular mechanisms by which small BL-induced conformational changes in the LOV2 domain are transmitted to the kinase remain unclear. Here, we used full-length wild-type and mutant phot2 proteins from
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Registered trials
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