ArticleNature communications2024
A c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.
What it found
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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.
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.
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Who cites it
33 citing papers in PubMed, 36 citations in OpenAlex.
- Biofilm-mediated antibiotic tolerance in bacterial pathogens: Integrated molecular networks and novel therapeutic avenues.Virulence · 2026Review
- Co-Expression of PA0290 and PelD EnhancesMicroorganisms · 2026Article
- Interaction of the polar localization protein BscR with phosphodiesterase PipA regulates virulence strategies in Pseudomonas aeruginosa.Journal of advanced research · 2026Article
- Roles of divalent metals in the regulation of cyclic di-GMP signaling in bacteria.Journal of bacteriology · 2026Review
- Article
- The versatility of the CHASE domain in one-component systems of c-di-GMP signal transduction fromJournal of bacteriology · 2026Article
- Biological and clinical significance of iron inJournal of bacteriology · 2026Review
- c-di-GMP is a key regulator of Pseudomonas aeruginosa response to UVA radiation.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026Article
- Single-bacterial cell insights into mechanisms of ceftriaxone resistance in Neisseria subflava.Nature communications · 2026Article
- Oxygen-responsive KoBdcA/KoBdcB/KoBpdA system regulates c-di-GMP levels to control bacterial cellulose biosynthesis and motility inMicrobiology spectrum · 2026Article
- Toolbox of FRET-based c-di-GMP biosensors and its FRET-To-Sort application for genome-wide mapping of c-di-GMP regulation.Nature communications · 2026Article
- Free ammonia stress rewires microbial signaling networks and constrains metabolic cooperation in oxygenic photogranules.The ISME journal · 2026Article
- Identification of key targets driving biofilm formation and virtual screening of potential inhibitors inFrontiers in microbiology · 2026Article
- Transcriptional profiling ofFrontiers in microbiology · 2026Article
- Diverse Biological Functions and Domain-Specific Interactions of the Diguanylate Cyclase PA2072 inInternational journal of microbiology · 2026Article
- Ferroptosis and iron-based therapies inVirulence · 2025Review
- Article
- eATP sensing by the purinergic receptor PA2072 for allosteric modulation in intracellular c-di-GMP signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dispersal Mechanisms in Biofilm Control: Characteristics, Induction, Impacts, and Therapeutic Potential.Current microbiology · 2025Review
- Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Cyclic dimeric guanosine monophosphate (c-di-GMP) serves as a bacterial second messenger that modulates various processes including biofilm formation, motility, and host-microbe symbiosis. Numerous studies have conducted comprehensive analysis of c-di-GMP. However, the mechanisms by which certain environmental signals such as iron control intracellular c-di-GMP levels are unclear. Here, we show that iron regulates c-di-GMP levels in Pseudomonas aeruginosa by modulating the interaction between an iron-sensing protein, IsmP, and a diguanylate cyclase, ImcA. Binding of iron to the CHASE4 domain of IsmP inhibits the IsmP-ImcA interaction, which leads to increased c-di-GMP synthesis by ImcA, thus promoting biofilm formation and reducing bacterial motility. Structural characterization of the apo-CHASE4 domain and its binding to iron allows us to pinpoint residues defining its specificity. In addition, the cryo-electron microscopy structure of ImcA in complex with a c-di-GMP analog (GMPCPP) suggests a unique conformation in which the compound binds to the catalytic pockets and to the membrane-proximal side located at the cytoplasm. Thus, our results indicate that a CHASE4 domain directly senses iron and modulates the crosstalk between c-di-GMP metabolic enzymes.
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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.