ArticleNature structural & molecular biology2024
Transport mechanism of presynaptic high-affinity choline uptake by CHT1.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- The sleep-wake cycle: molecular mechanisms, disorders, and therapeutic targets in the context of energy metabolism.Signal transduction and targeted therapy · 2026Review
- Differential recruitment of acetylcholine vesicle pools by electrical stimulation and KCl depolarization in cholinergic nerve terminals.FEBS letters · 2026Article
- Structural and biochemical comparison of the FLVCR and CTL membrane protein families in eukaryotes.Life science alliance · 2026Article
- Structural basis for multivitamin recognition and transport by human SMVT.Nature communications · 2026Article
- Structural insights into a conserved mechanism of choline translocation through CHT.Science advances · 2026Article
- Structural insight into the glucose-6-phosphate transport by G6PT1 and inhibition mechanism of CGA.Science advances · 2026Article
- The Central Cholinergic Synapse: A Primer.International journal of molecular sciences · 2025Review
- The Roles of Acetylcholine and Muscarinic Receptors in Allergic Rhinitis: Mechanisms, Clinical Insights and Future Directions.Current allergy and asthma reports · 2025Review
- Cryo-EM ligand building using AlphaFold3-like model and molecular dynamics.PLoS computational biology · 2025Article
- Review
- Structural basis of urea transport by Arabidopsis thaliana DUR3.Nature communications · 2025Article
- Cellular and organismal function of choline metabolism.Nature metabolism · 2025Review
- Structural mechanisms of human sodium-coupled high-affinity choline transporter CHT1.Cell discovery · 2024Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Choline is a vital nutrient and a precursor for the biosynthesis of essential metabolites, including acetylcholine (ACh), that play a central role in fetal development, especially in the brain. In cholinergic neurons, the high-affinity choline transporter (CHT1) provides an extraordinarily efficient reuptake mechanism to reutilize choline derived from intrasynaptical ACh hydrolysis and maintain ACh synthesis in the presynapse. Here, we determined structures of human CHT1 in three discrete states: the outward-facing state bound with the competitive inhibitor hemicholinium-3 (HC-3); the inward-facing occluded state bound with the substrate choline; and the inward-facing apo open state. Our structures and functional characterizations elucidate how the inhibitor and substrate are recognized. Moreover, our findings shed light on conformational changes when transitioning from an outward-facing to an inward-facing state and establish a framework for understanding the transport cycle, which relies on the stabilization of the outward-facing state by a short intracellular helix, IH1.
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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.