ArticleThe Journal of biological chemistry2019
Dopamine transporter forms stable dimers in the live cell plasma membrane in a phosphatidylinositol 4,5-bisphosphate-independent manner.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Cell membrane cholesterol affects serotonin transporter efflux due to altered transporter oligomerization.Molecular psychiatry · 2026Article
- Dimerization and substrate recognition of human taurine transporter.Nature communications · 2025Article
- Functional neuroanatomy of dopaminergic arousal systems: implications for the wake-promoting effect of psychostimulants, with particular reference to modafinil.Frontiers in neuroanatomy · 2025Review
- Review
- Oligomerization of Monoamine Transporters.Sub-cellular biochemistry · 2024Review
- Monte Carlo simulations for the evaluation of oligomerization data in TOCCSL experiments.Biophysical journal · 2023Article
- Overview of the structure and function of the dopamine transporter and its protein interactions.Frontiers in physiology · 2023Review
- A comparative review on the well-studied GAT1 and the understudied BGT-1 in the brain.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
- Phosphatidylinositol 4,5-bisphosphate (PIPCommunications biology · 2022Article
- Nanoscopic dopamine transporter distribution and conformation are inversely regulated by excitatory drive and D2 autoreceptor activity.Cell reports · 2022Article
- Insights into the Role of Membrane Lipids in the Structure, Function and Regulation of Integral Membrane Proteins.International journal of molecular sciences · 2021Review
- SLC6 transporter oligomerization.Journal of neurochemistry · 2021Review
- Dynamic control of the dopamine transporter in neurotransmission and homeostasis.NPJ Parkinson's disease · 2021Review
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Trimerization of dopamine transporter triggered by AIM-100 binding: Molecular mechanism and effect of mutations.Neuropharmacology · 2019Article
- Monoamine transporters: structure, intrinsic dynamics and allosteric regulation.Nature structural & molecular biology · 2019Review
- Structure and Gating Dynamics of NaFrontiers in molecular biosciences · 2019Review
- It takes two-or more-to tango: Revisiting the role of dopamine transporter oligomerization.The Journal of biological chemistryArticle
- Optogenetically-induced multimerization of the dopamine transporter increases uptake and trafficking to the plasma membrane.The Journal of biological chemistryArticle
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7 authors.
Funding
Abstract
The human dopamine transporter (hDAT) regulates the level of the neurotransmitter dopamine (DA) in the synaptic cleft and recycles DA for storage in the presynaptic vesicular pool. Many neurotransmitter transporters exist as oligomers, but the physiological role of oligomerization remains unclear; for example, it has been speculated to be a prerequisite for amphetamine-induced release and protein trafficking. Previous studies point to an oligomeric quaternary structure of hDAT; however, the exact stoichiometry and the fraction of co-existing oligomeric states are not known. Here, we used single-molecule brightness analysis to quantify the degree of oligomerization of heterologously expressed hDAT fused to monomeric GFP (mGFP-hDAT) in Chinese hamster ovary (CHO) cells. We observed that monomers and dimers of mGFP-hDAT co-exist and that higher-order molecular complexes of mGFP-hDAT are absent at the plasma membrane. The mGFP-hDAT dimers were stable over several minutes, and the fraction of dimers was independent of the mGFP-hDAT surface density. Furthermore, neither oxidation nor depletion of cholesterol had any effect on the fraction of dimers. Unlike for the human serotonin transporter (hSERT), in which direct binding of phosphatidylinositol 4,5-bisphosphate (PIP
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