ArticleScience signaling2011
Structure of a light-activated LOV protein dimer that regulates transcription.
Article in Science signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
77 citing papers in PubMed, 135 citations in OpenAlex.
- Article
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- Trends in circadian rhythms research in fungi since the millenium.Npj biological timing and sleep · 2026Review
- Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026Article
- Enhancing the performance of Magnets photosensors.Nature communications · 2026Article
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Red-Light-Only Control of Protein-Protein Interactions Using a Cyanobacteriochrome (UNICYCL).ACS central science · 2026Article
- How fungi see the world: fungal photoreceptors and their role in the regulation of fungal biology.Microbiology and molecular biology reviews : MMBR · 2025Review
- Bayesian Nonparametric Analysis of Residence Times for Protein-Lipid Interactions in Molecular Dynamics Simulations.Journal of chemical theory and computation · 2025Article
- Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222.Nucleic acids research · 2025Article
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation.Journal of visualized experiments : JoVE · 2024Article
- Dimerization activates the Inversin complex inMolecular biology of the cell · 2024Article
- Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- Reduction midpoint potential of a paradigm light-oxygen-voltage receptor and its modulation by methionine residues.RSC chemical biology · 2024Article
- Opticool: Cutting-edge transgenic optical tools.PLoS genetics · 2024Review
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- Origin and functional diversification of PAS domain, a ubiquitous intracellular sensor.Science advances · 2023Article
- An Anatomy of Fungal Eye: Fungal Photoreceptors and Signalling Mechanisms.Journal of fungi (Basel, Switzerland) · 2023Review
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Light, oxygen, or voltage (LOV) protein domains are present in many signaling proteins in bacteria, archaea, protists, plants, and fungi. The LOV protein VIVID (VVD) of the filamentous fungus Neurospora crassa enables the organism to adapt to constant or increasing amounts of light and facilitates proper entrainment of circadian rhythms. Here, we determined the crystal structure of the fully light-adapted VVD dimer and reveal the mechanism by which light-driven conformational change alters the oligomeric state of the protein. Light-induced formation of a cysteinyl-flavin adduct generated a new hydrogen bond network that released the amino (N) terminus from the protein core and restructured an acceptor pocket for binding of the N terminus on the opposite subunit of the dimer. Substitution of residues critical for the switch between the monomeric and the dimeric states of the protein had profound effects on light adaptation in Neurospora. The mechanism of dimerization of VVD provides molecular details that explain how members of a large family of photoreceptors convert light responses to alterations in protein-protein interactions.
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Registered trials
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.