ArticleNature communications2025
Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed.
- Genome assembly and comparative genomic analysis of the extracellular polysaccharide-overproducing strain Schizophyllum commune SC-N.World journal of microbiology & biotechnology · 2026Article
- The Structure, Biosynthesis, and Function of β-1,6-Glucan in the Fungal Cell Wall.Biomolecules · 2026Review
- A bipartite glucan synthase-remodeler module organizes branched glucan assembly in the fungal cell wall.Nature communications · 2026Article
- Article
- Mutational landscape and molecular bases of echinocandin resistance in Saccharomyces cerevisiae.Genetics · 2026Article
- Small Molecular Peptides and Their Potential Antifungal Activities During the Pile-Fermentation of Post-Fermented Tea.Foods (Basel, Switzerland) · 2026Article
- Deciphering the multidrug resistance paradigm inAntimicrobial agents and chemotherapy · 2026Review
- Inhibition mechanism of the fungal β-1,3-glucan synthases by triterpenoid antifungal drugs.Nature communications · 2026Article
- Immune Responses toJournal of inflammation research · 2026Review
- Structural-guided identification of two modulators of β-1,3-glucan synthase FKS1.Nature communications · 2025Article
- Computational Approaches for Discovering Virulence Factors inJournal of fungi (Basel, Switzerland) · 2025Review
- Molecular landscape of the fungal plasma membrane and implications for antifungal action.Nature communications · 2025Article
- The Ync13-Rga7-Rng10 complex selectively coordinates secretory vesicle trafficking and secondary septum formation during cytokinesis.PLoS biology · 2025Article
- Spatial control of secretory vesicle targeting by the Ync13-Rga7-Rng10 complex during cytokinesis.bioRxiv : the preprint server for biology · 2025Article
- The phenomenon of anhydrobiosis-structural and functional changes in yeast cells.Applied microbiology and biotechnology · 2025Review
- Targeting epigenetic regulators to overcome drug resistance in the emerging human fungal pathogen Candida auris.Nature communications · 2025Article
- Fungal β-1,3-glucan synthase: a review of structure, mechanism, and regulation.FEMS yeast research · 2025Review
- New antifungal strategies and drug development against WHO critical priority fungal pathogens.Frontiers in cellular and infection microbiology · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-1,3 Glucan synthase (GS) is essential for fungal cell wall biosynthesis. The GS holoenzyme comprises the glycosyltransferase FKS1 and its regulatory factor Rho1, a small GTPase. However, the mechanism by which Rho1 activates FKS1 in a GTP-dependent manner remains unclear. Here, we present two cryo-EM structures of FKS1, apo and in complex with Rho1. FKS1 adopts a cellulose synthase-like conformation. The interaction between Rho1 and FKS1 is enhanced in the presence of GTPγS. Rho1 is positioned within a pocket between the glycosyltransferase domain of FKS1 (GT domain) and the transmembrane helix spanning TM7-15. Comparison of the two structures reveals extensive conformational changes within FKS1. These alterations suggest that Rho1's GTP/GDP cycling may act as a molecular pump, promoting a dynamic transition between the resting and active states of FKS1. Notably, Rho1 triggers FKS1 conformational changes that may push the growing glucan chain into FKS1's transmembrane channel, thereby facilitating β-1,3-glucan elongation.
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.