ArticleNature communications2024
Neurotransmitter recognition by human vesicular monoamine transporter 2.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Development and characterization of a reserpine-induced mouse model of depression: An integrated in-vivo and in-silico approach.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Structural studies and functional engineering of NanX: an anhydro-sialic acid transporter from Escherichia coli.FEBS open bio · 2026Article
- Post-mortem brain analysis reveals altered monoaminergic system in the dorsolateral prefrontal cortex and hippocampus in chronic schizophrenia.Schizophrenia (Heidelberg, Germany) · 2026Article
- Biological Breakthroughs and Drug Discovery Revolution via Cryo-Electron Microscopy of Membrane Proteins.Membranes · 2025Review
- Ultralow-Power Peptide-Based Memristor Enabled by Emulation of Proton-Mediated Synaptic Signaling.Small methods · 2025Article
- Enterococcus faecalis SI-FC-01 enhances the stress resistance and healthspan of C. elegans via AKT signaling pathway.Scientific reports · 2025Article
- Drug inhibition and substrate transport mechanisms of human VMAT2.Nature communications · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Human vesicular monoamine transporter 2 (VMAT2), a member of the SLC18 family, plays a crucial role in regulating neurotransmitters in the brain by facilitating their uptake and storage within vesicles, preparing them for exocytotic release. Because of its central role in neurotransmitter signalling and neuroprotection, VMAT2 is a target for neurodegenerative diseases and movement disorders, with its inhibitor being used as therapeutics. Despite the importance of VMAT2 in pharmacophysiology, the molecular basis of VMAT2-mediated neurotransmitter transport and its inhibition remains unclear. Here we show the cryo-electron microscopy structure of VMAT2 in the substrate-free state, in complex with the neurotransmitter dopamine, and in complex with the inhibitor tetrabenazine. In addition to these structural determinations, monoamine uptake assays, mutational studies, and pKa value predictions were performed to characterize the dynamic changes in VMAT2 structure. These results provide a structural basis for understanding VMAT2-mediated vesicular transport of neurotransmitters and a platform for modulation of current inhibitor design.
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