ArticleProceedings of the National Academy of Sciences of the United States of America1999
LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers.
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Who cites it
212 citing papers in PubMed, 567 citations in OpenAlex.
- QM/MM Calculated Triplet-Singlet Infrared Difference Spectra of LOV2 Photoreceptor Domains and FMN in Solution.ACS omega · 2026Article
- CD44 restricts EGFR mobility to polarize cytoskeletal signalling modules driving bleb-based migration.Nature cell biology · 2026Article
- Blue light receptor phot2 collaborates with NRL-30 to negatively regulate immunity by reducing mitochondrial protein PRXIIF stability in potato.Molecular horticulture · 2026Article
- Lights up on the embryonic dance: tools and applications of optogenetics in developmental biology.Genes & development · 2026Review
- Protein Electrostatics Tune the Singlet-Triplet Energy Gap in Natural and Engineered Phototropin Light-Oxygen-Voltage (LOV) Domains.Journal of the American Chemical Society · 2026Article
- Article
- How fungi see the world: fungal photoreceptors and their role in the regulation of fungal biology.Microbiology and molecular biology reviews : MMBR · 2025Review
- Histone deacetylase 9 modulates the acetylation dynamics of phototropin 1 to fine-tune phototropic responses in plants.Plant communications · 2025Article
- Emerging roles of transcriptional condensates as temporal signal integrators.Nature reviews. Genetics · 2025Review
- Photo-CIDNP of Solvent-Exposed Flavins in Flavoproteins.The journal of physical chemistry letters · 2025Article
- Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications.Biochemistry · 2025Review
- POT, an optogenetics-based endogenous protein degradation system.Communications biology · 2025Article
- The role of blue light in plant stress responses: modulation through photoreceptors and antioxidant mechanisms.Frontiers in plant science · 2025Review
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Electronic Structure Methods for Simulating Flavin's Spectroscopy and Photophysics: Comparison of Multi-reference, TD-DFT, and Single-Reference Wave Function Methods.The journal of physical chemistry. B · 2024Article
- Turn-on protein switches for controlling actin binding in cells.Nature communications · 2024Article
- Current advances in photocatalytic proximity labeling.Cell chemical biology · 2024Review
- Elucidating the Signal Transduction Mechanism of the Blue-Light-Regulated Photoreceptor YtvA: From Photoactivation to Downstream Regulation.ACS chemical biology · 2024Article
- Optical Approaches for Investigating Neuromodulation and G Protein-Coupled Receptor Signaling.Pharmacological reviews · 2023Review
- Optogenetic control of YAP reveals a dynamic communication code for stem cell fate and proliferation.Nature communications · 2023Article
152 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phototropism, the bending response of plant organs to or away from a directional light source, is one of the best studied blue light responses in plants. Although phototropism has been studied for more than a century, recent advances have improved our understanding of the underlying signaling mechanisms involved. The NPH1 gene of Arabidopsis thaliana encodes a blue light-dependent autophosphorylating protein kinase with the properties of a photoreceptor for phototropism. NPH1 apoprotein noncovalently binds FMN to form the holoprotein nph1. The N-terminal region of the protein contains two LOV (light, oxygen, or voltage) domains that share homology with sensor proteins from a diverse group of organisms. These include the bacterial proteins NIFL and AER, both of which bind FAD, and the phy3 photoreceptor from Adiantium capillus-veneris. The LOV domain has therefore been proposed to reflect a flavin-binding site, regulating nph1 kinase activity in response to blue light-induced redox changes. Herein we demonstrate that the LOV domains of two nph1 proteins and phy3 bind stoichiometric amounts of FMN when expressed in Escherichia coli. The spectral properties of the chromopeptides are similar to the action spectrum for phototropism, implying that the LOV domain binds FMN to function as a light sensor. Thus, our findings support the earlier model that nph1 is a dual-chromophoric flavoprotein photoreceptor regulating phototropic responses in higher plants. We therefore propose the name phototropin to designate the nph1 holoprotein.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.