ArticleThe Journal of biological chemistry2013
Charting the signal trajectory in a light-oxygen-voltage photoreceptor by random mutagenesis and covariance analysis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- Framework for Quantifying the Efficiency of Competing Signal Transmission Modes in Proteins.Journal of the American Chemical Society · 2026Article
- Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.Nature communications · 2024Article
- Light-regulated gene expression in Bacteria: Fundamentals, advances, and perspectives.Frontiers in bioengineering and biotechnology · 2022Review
- Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling.Nature communications · 2021Article
- Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019Review
- Synthetic cell-like membrane interfaces for probing dynamic protein-lipid interactions.Methods in enzymology · 2019Article
- Blue-Light Receptors for Optogenetics.Chemical reviews · 2018Review
- Directly light-regulated binding of RGS-LOV photoreceptors to anionic membrane phospholipids.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Blue-light reception through quaternary transitions.Scientific reports · 2017Article
- Signal transduction in light-oxygen-voltage receptors lacking the adduct-forming cysteine residue.Nature communications · 2015Article
- 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
- Photoreceptor engineering.Frontiers in molecular biosciences · 2015Review
- LOV-based optogenetic devices: light-driven modules to impart photoregulated control of cellular signaling.Frontiers in molecular biosciences · 2015Review
- Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Photo-sensitive degron variants for tuning protein stability by light.BMC systems biology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modular signal receptors empower organisms to process environmental stimuli into adequate physiological responses. At the molecular level, a sensor module receives signals and processes the inherent information into changes of biological activity of an effector module. To better understand the molecular bases underpinning these processes, we analyzed signal reception and processing in the dimeric light-oxygen-voltage (LOV) blue light receptor YF1 that serves as a paradigm for the widespread Per-ARNT-Sim (PAS) signal receptors. Random mutagenesis identifies numerous YF1 variants in which biological activity is retained but where light regulation is abolished or inverted. One group of variants carries mutations within the LOV photosensor that disrupt proper coupling of the flavin-nucleotide chromophore to the protein scaffold. Another larger group bears mutations that cluster at the dyad interface and disrupt signal transmission to two coaxial coiled-coils that connect to the effector. Sequence covariation implies wide conservation of structural and mechanistic motifs, as also borne out by comparison to several PAS domains in which mutations leading to disruption of signal transduction consistently map to confined regions broadly equivalent to those identified in YF1. Not only do these data provide insight into general mechanisms of signal transduction, but also they establish concrete means for customized reprogramming of signal receptors.
Indexed as
Identifiers
What OpenQuestion holds
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.