ArticleProceedings of the National Academy of Sciences of the United States of America2001
Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 217 citations in OpenAlex.
- Single-molecule fluorescence and cross-linking reveal ligand-gated Toc34 oligomerization dynamics.Biophysical journal · 2026Article
- Regulation of Dopamine Transporter Surface Expression.Advances in neurobiology · 2025Review
- A Conserved Intramolecular Ion-Pair Plays a Critical but Divergent Role in Regulation of Dimerization and Transport Function among the Monoamine Transporters.International journal of molecular sciences · 2024Article
- Oligomerization of Monoamine Transporters.Sub-cellular biochemistry · 2024Review
- Structures and membrane interactions of native serotonin transporter in complexes with psychostimulants.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Overview of the structure and function of the dopamine transporter and its protein interactions.Frontiers in physiology · 2023Review
- Cross-Linking and Functional Analyses for Dimerization of a Cysteine Mutant of Glycine Transporter 1.International journal of molecular sciences · 2022Article
- SLC6 transporter oligomerization.Journal of neurochemistry · 2021Review
- Dynamic control of the dopamine transporter in neurotransmission and homeostasis.NPJ Parkinson's disease · 2021Review
- Effect of palmitoylation on the dimer formation of the human dopamine transporter.Scientific reports · 2021Article
- Cocaine analogue conjugated magnetic nanoparticles for labeling and imaging dopaminergic neurons.Biomaterials science · 2020Article
- Trimerization of dopamine transporter triggered by AIM-100 binding: Molecular mechanism and effect of mutations.Neuropharmacology · 2019Article
- Dopamine transporter forms stable dimers in the live cell plasma membrane in a phosphatidylinositol 4,5-bisphosphate-independent manner.The Journal of biological chemistry · 2019Article
- Dopamine transporter oligomerization involves the scaffold domain, but spares the bundle domain.PLoS computational biology · 2018Article
- Article
- Dimer Interface of the Human Serotonin Transporter and Effect of the Membrane Composition.Scientific reports · 2018Article
- Amphetamine Reverses Escalated Cocaine Intake via Restoration of Dopamine Transporter Conformation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Linking Glycation and Glycosylation With Inflammation and Mitochondrial Dysfunction in Parkinson's Disease.Frontiers in neuroscience · 2018Review
- Functional properties of dopamine transporter oligomers after copper linking.Journal of neurochemistry · 2018Article
- Phosphorylation of the Amino Terminus of the Dopamine Transporter: Regulatory Mechanisms and Implications for Amphetamine Action.Advances in pharmacology (San Diego, Calif.) · 2018Review
17 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
There is evidence both for and against Na(+)- and Cl(-)-dependent neurotransmitter transporters forming oligomers. We found that cross-linking the human dopamine transporter (DAT), which is heterologously expressed in human embryonic kidney 293 cells, either with copper phenanthroline (CuP) or the bifunctional reagent bis-(2-methanethiosulfonatoethyl)amine hydrochloride (bis-EA) increased the apparent molecular mass determined with nonreducing SDS/PAGE from approximately 85 to approximately 195 kDa. After cross-linking, but not before, coexpressed, differentially epitope-tagged DAT molecules, solubilized in Triton X-100, were coimmunoprecipitated. Thus, the 195-kDa complex was a homodimer. Cross-linking of DAT did not affect tyramine uptake. Replacement of Cys-306 with Ala prevented cross-linking. Replacement of all of the non-disulfide-bonded cysteines in the extracellular and membrane domains, except for Cys-306, did not prevent cross-linking. We conclude that the cross-link is between Cys-306 at the extracellular end of TM6 in each of the two DATs. The motif GVXXGVXXA occurs at the intracellular end of TM6 in DAT and is found in a number of other neurotransmitter transporters. This sequence was originally found at the dimerization interface in glycophorin A, and it promotes dimerization in model systems. Mutation of either glycine disrupted DAT expression and function. The intracellular end of TM6, like the extracellular end, is likely to be part of the dimerization interface.
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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.