ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009
Physical and functional interaction between the dopamine transporter and the synaptic vesicle protein synaptogyrin-3.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 143 citations in OpenAlex.
- High-performance surface plasmon resonance sensor utilizing AuNPs/Au nanocone array for ultrasensitive dopamine detection in complex biological matrices.Mikrochimica acta · 2026Article
- Lactoperoxidase is a candidate for mediating neuromelanin formation in the human substantia nigra.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- SYNGR3 Accelerates α-Synuclein Aggregation and Neurodegeneration in Parkinson's Disease.CNS neuroscience & therapeutics · 2026Article
- Synaptogyrin-3 plays a critical role in addiction-related dopamine dysfunction and behavioral maladaptations.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Kappa opioid receptor antagonism restores phosphorylation, trafficking and behavior induced by a disease-associated dopamine transporter variant.Molecular psychiatry · 2025Article
- Melanin and Neurotransmitter Signalling Genes Are Differentially Co-Expressed in Growing Feathers of White and Rufous Barn Owls.Pigment cell & melanoma research · 2025Article
- Neurotoxicology of dopamine: Victim or assailant?Neurotoxicology · 2024Review
- The association of genetic polymorphisms within the dopaminergic system with nicotine dependence: A narrative review.Heliyon · 2024Review
- Targets to Search for New Pharmacological Treatment in Idiopathic Parkinson's Disease According to the Single-Neuron Degeneration Model.Biomolecules · 2024Review
- Molecular Dynamic Simulations to Determine Individualized Therapy: Tetrabenazine for the GNAO1 Encephalopathy E246K Variant.Molecular diagnosis & therapy · 2024Article
- Oligomerization of Monoamine Transporters.Sub-cellular biochemistry · 2024Review
- Article
- In vivo overexpression of synaptogyrin-3 promotes striatal synaptic dopamine uptake in LRRK2Brain and behavior · 2023Article
- The endogenous cannabinoid system modulates male sexual behavior expression.Frontiers in behavioral neuroscience · 2023Review
- Identification of Hub Genes and Potential Molecular Pathogenesis in Substantia Nigra in Parkinson's Disease via Bioinformatics Analysis.Parkinson's disease · 2023Article
- Tumor Cell Extrinsic Synaptogyrin 3 Expression as a Diagnostic and Prognostic Biomarker in Head and Neck Cancer.Cancer research communications · 2022Article
- Betel quid: New insights into an ancient addiction.Addiction biology · 2022Article
- A density-based enrichment measure for assessing colocalization in single-molecule localization microscopy data.Nature communications · 2022Article
- Divergent properties and independent regulation of striatal dopamine and GABA co-transmission.Cell reports · 2022Article
- Transcriptional Regulation of the Synaptic Vesicle Protein Synaptogyrin-3 (International journal of molecular sciences · 2022Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
Uptake through the dopamine transporter (DAT) represents the primary mechanism used to terminate dopaminergic transmission in brain. Although it is well known that dopamine (DA) taken up by the transporter is used to replenish synaptic vesicle stores for subsequent release, the molecular details of this mechanism are not completely understood. Here, we identified the synaptic vesicle protein synaptogyrin-3 as a DAT interacting protein using the split ubiquitin system. This interaction was confirmed through coimmunoprecipitation experiments using heterologous cell lines and mouse brain. DAT and synaptogyrin-3 colocalized at presynaptic terminals from mouse striatum. Using fluorescence resonance energy transfer microscopy, we show that both proteins interact in live neurons. Pull-down assays with GST (glutathione S-transferase) proteins revealed that the cytoplasmic N termini of both DAT and synaptogyrin-3 are sufficient for this interaction. Furthermore, the N terminus of DAT is capable of binding purified synaptic vesicles from brain tissue. Functional assays revealed that synaptogyrin-3 expression correlated with DAT activity in PC12 and MN9D cells, but not in the non-neuronal HEK-293 cells. These changes were not attributed to changes in transporter cell surface levels or to direct effect of the protein-protein interaction. Instead, the synaptogyrin-3 effect on DAT activity was abolished in the presence of the vesicular monoamine transporter-2 (VMAT2) inhibitor reserpine, suggesting a dependence on the vesicular DA storage system. Finally, we provide evidence for a biochemical complex involving DAT, synaptogyrin-3, and VMAT2. Collectively, our data identify a novel interaction between DAT and synaptogyrin-3 and suggest a physical and functional link between DAT and the vesicular DA system.
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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.