ArticleNature structural & molecular biology2025
Binding mechanism and antagonism of the vesicular acetylcholine transporter VAChT.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Advances in Targeting Central Cholinergic Dysfunction for Neurodegenerative Diseases: From Pharmacotherapy to Neuromodulation.CNS neuroscience & therapeutics · 2026Review
- Insecticidal effects of oxazosulfyl result from synaptic inhibition by targeting the vesicular acetylcholine transporter.Journal of pesticide science · 2026Article
- Mild photothermal therapy ameliorates neurogenic bladder after sacral spinal cord injury via multi-target effects.Materials today. Bio · 2026Article
- Varenicline-mediated cholinergic activation through α4β2 nAChR inhibits microglial neuroinflammation and alleviates neuropathic pain and depression following spinal cord injury.Journal of translational medicine · 2026Article
- Neurotransmitter Dysregulation in Parkinson's Disease: Pathophysiological Insights and Therapeutic Perspectives.ACS chemical neuroscience · 2026Review
- Structural insight into the glucose-6-phosphate transport by G6PT1 and inhibition mechanism of CGA.Science advances · 2026Article
- Cardiac endogenous transmitter system: molecular features, functions, and clinical implications.European heart journal · 2026Review
- A taxon-centered review of bacterial shifts in psychiatric disorders.Frontiers in psychiatry · 2026Review
- The Central Cholinergic Synapse: A Primer.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vesicular acetylcholine transporter (VAChT) has a pivotal role in packaging and transporting acetylcholine for exocytotic release, serving as a vital component of cholinergic neurotransmission. Dysregulation of its function can result in neurological disorders. It also serves as a target for developing radiotracers to quantify cholinergic neuron deficits in neurodegenerative conditions. Here we unveil the cryo-electron microscopy structures of human VAChT in its apo state, the substrate acetylcholine-bound state and the inhibitor vesamicol-bound state. These structures assume a lumen-facing conformation, offering a clear depiction of architecture of VAChT. The acetylcholine-bound structure provides a detailed understanding of how VAChT recognizes its substrate, shedding light on the coupling mechanism of protonation and substrate binding. Meanwhile, the vesamicol-bound structure reveals the binding mode of vesamicol to VAChT, laying the structural foundation for the design of the next generation of radioligands targeting VAChT.
Indexed as
Identifiers
39806024What 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.