ArticleStructure (London, England : 1993)2022
Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- CcTRP1, a Putative TRP Channel in Cordyceps cicadae, Regulates Hyphal Growth, Stress Responses, and Bioactive Metabolite Biosynthesis.Current microbiology · 2026Article
- Artificial intelligence using a latent diffusion model enables the generation of diverse and potent antimicrobial peptides.Science advances · 2025Article
- Advances in the cellular biology, biochemistry, and molecular biology of acidocalcisomes.Microbiology and molecular biology reviews : MMBR · 2024Review
- The versatility of the putative transient receptor potential ion channels in regulating the calcium signaling inmSphere · 2023Article
- Calcium Ion Channels inJournal of fungi (Basel, Switzerland) · 2023Review
- Membrane-anchored calpains - hidden regulators of growth and development beyond plants?Frontiers in plant science · 2023Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Calmodulin kinase 2 genetically interacts with Rch1p to negatively regulate calcium import into Saccharomyces cerevisiae after extracellular calcium pulse.Archives of microbiology · 2022Article
- A Transient Receptor Potential-like Calcium Ion Channel in the Filamentous FungusJournal of fungi (Basel, Switzerland) · 2021Article
- Druggable Lipid Binding Sites in Pentameric Ligand-Gated Ion Channels and Transient Receptor Potential Channels.Frontiers in physiology · 2021Review
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6 authors at 2 institutions in 1 country.
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Abstract
Transient receptor potential (TRP) channels emerged in fungi as mechanosensitive osmoregulators. The Saccharomyces cerevisiae vacuolar TRP yeast 1 (TRPY1) is the most studied TRP channel from fungi, but the structure and details of channel modulation remain elusive. Here, we describe the full-length cryoelectron microscopy structure of TRPY1 at 3.1 Å resolution in a closed state. The structure, despite containing an evolutionarily conserved and archetypical transmembrane domain, reveals distinctive structural folds for the cytosolic N and C termini, compared with other eukaryotic TRP channels. We identify an inhibitory phosphatidylinositol 3-phosphate (PI(3)P) lipid-binding site, along with two Ca
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