ArticleJournal of neurochemistry2015
Dopamine transporter oligomerization: impact of combining protomers with differential cocaine analog binding affinities.
Article in Journal of neurochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 36 citations in OpenAlex.
- Cocaine Use Disorder: Neuropathology and Exploratory Treatments.Molecular neurobiology · 2026Review
- Hypocretin / Orexin Receptor 1 Knockdown in GABA or Dopamine Neurons in the Ventral Tegmental Area Differentially Impact Mesolimbic Dopamine and Motivation for Cocaine.Addiction neuroscience · 2023Article
- Overview of the structure and function of the dopamine transporter and its protein interactions.Frontiers in physiology · 2023Review
- UV and temperature effects on chloroacetanilide and triazine herbicides degradation and cytotoxicity.Heliyon · 2021Article
- Association of sigma-1 receptor with dopamine transporter attenuates the binding of methamphetamine via distinct helix-helix interactions.Chemical biology & drug design · 2021Article
- SLC6 transporter oligomerization.Journal of neurochemistry · 2021Review
- Dynamic control of the dopamine transporter in neurotransmission and homeostasis.NPJ Parkinson's disease · 2021Review
- Dopamine transporter function fluctuates across sleep/wake state: potential impact for addiction.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2021Article
- Identification of a New Allosteric Binding Site for Cocaine in Dopamine Transporter.Journal of chemical information and modeling · 2020Article
- 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
- Tales of tails in transporters.Open biology · 2019Review
- Palmitoylation by Multiple DHHC Enzymes Enhances Dopamine Transporter Function and Stability.ACS chemical neuroscience · 2019Article
- Model systems for analysis of dopamine transporter function and regulation.Neurochemistry international · 2019Review
- 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
- Functional properties of dopamine transporter oligomers after copper linking.Journal of neurochemistry · 2018Article
- Palmitoylation mechanisms in dopamine transporter regulation.Journal of chemical neuroanatomy · 2017Review
- Allosteric modulation of human dopamine transporter activity under conditions promoting its dimerization.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Previous studies point to quaternary assembly of dopamine transporters (DATs) in oligomers. However, it is not clear whether the protomers function independently in the oligomer. Is each protomer an entirely separate unit that takes up dopamine and is inhibited by drugs known to block DAT function? In this work, human embryonic kidney 293 cells were co-transfected with DAT constructs possessing differential binding affinities for the phenyltropane cocaine analog, [³H]WIN35,428. It was assessed whether the binding properties in co-expressing cells capable of forming hetero-oligomers differ from those in preparations obtained from mixed singly transfected cells where such oligomers cannot occur. A method is described that replaces laborious 'mixing' experiments with an in silico method predicting binding parameters from those observed for the singly expressed constructs. Among five pairs of constructs tested, statistically significant interactions were found between protomers of wild-type (WT) and D313N, WT and D345N, and WT and D436N. Compared with predicted Kd values of [³H]WIN35,428 binding to the non-interacting pairs, the observed affinity of the former pair was increased 1.7 fold while the latter two were reduced 2.2 and 4.1 fold, respectively. This is the first report of an influence of protomer composition on the properties of a DAT inhibitor, indicating cooperativity within the oligomer. The dopamine transporter (DAT) can exist as an oligomer but it is unknown whether the protomers function independently. The present results indicate that protomers that are superpotent or deficient in cocaine analog binding can confer enhanced or reduced potency to the oligomer, respectively. In this respect, positive or negative cooperativity is revealed in the DAT oligomer.
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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.