ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2008
Currents in response to rapid concentration jumps of amphetamine uncover novel aspects of human dopamine transporter function.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 67 citations in OpenAlex.
- The Role of Cholesterol at the CHOL2 Site and the Dimeric Interface in the Regulation of Serotonin Transporter Function and Dimerization.Biomolecules · 2026Article
- Electrophysiological Methods to Explore the Function of Monoamine Transporters.Advances in neurobiology · 2025Review
- Structural and functional perspectives on interactions between synthetic cathinones and monoamine transporters.Advances in pharmacology (San Diego, Calif.) · 2024Article
- Persistent binding at dopamine transporters determines sustained psychostimulant effects.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Elucidating the Mechanism Behind Sodium-Coupled Neurotransmitter Transporters by Reconstitution.Neurochemical research · 2022Review
- Handling of intracellular KeLife · 2021Article
- Descriptors of Secondary Active Transporter Function and How They Relate to Partial Reactions in the Transport Cycle.Membranes · 2021Article
- Bile Acids Gate Dopamine Transporter Mediated Currents.Frontiers in chemistry · 2021Article
- Allosteric Modulation of Neurotransmitter Transporters as a Therapeutic Strategy.Trends in pharmacological sciences · 2020Review
- Maternal Immune Activation and the Development of Dopaminergic Neurotransmission of the Offspring: Relevance for Schizophrenia and Other Psychoses.Frontiers in psychiatry · 2020Review
- Article
- Kinetic Models of Secondary Active Transporters.International journal of molecular sciences · 2019Article
- A comparison of the transport kinetics of glycine transporter 1 and glycine transporter 2.The Journal of general physiology · 2019Article
- 2-Aminoindan and its ring-substituted derivatives interact with plasma membrane monoamine transporters and αPsychopharmacology · 2019Article
- Using CaPsychopharmacology · 2019Review
- Structural, functional, and behavioral insights of dopamine dysfunction revealed by a deletion inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- An unsuspected role for organic cation transporter 3 in the actions of amphetamine.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018Article
- A kinetic account for amphetamine-induced monoamine release.The Journal of general physiology · 2018Article
- The N Terminus Specifies the Switch between Transport Modes of the Human Serotonin Transporter.The Journal of biological chemistry · 2017Article
- Electrogenic Binding of Intracellular Cations Defines a Kinetic Decision Point in the Transport Cycle of the Human Serotonin Transporter.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Amphetamine (AMPH) is a widely abused psychostimulant that acts as a substrate for the human dopamine transporter (hDAT). Using a piezoelectric rapid application system, we measured AMPH-induced currents mediated by hDAT. Whole-cell patch-clamp recordings in a heterologous expression system reveal that AMPH induces a rapidly activating and subsequently decaying inward current mediated by hDAT. We hypothesize that this transient inward current reflects a conformational change associated with substrate translocation. The AMPH-induced current strictly depends on extracellular Na+. Elevated intracellular Na+ has no effect on the peak AMPH-induced current amplitude but inhibits the steady-state current. In addition, elevated intracellular Na+ causes an overshoot outward current upon washout of AMPH that reflects hDAT locked in a Na+-exchange mode. Furthermore, elevated intracellular Na+ dramatically accelerates the recovery time from desensitization of the AMPH-induced current, revealing a new role for intracellular Na+ in promoting the transition to the hDAT "outward-facing" conformation. Ion substitution suggests that both extracellular and intracellular Cl- facilitate transporter turnover in contrast to the classical model of Cl- as a cotransported ion. We present an alternating-access model of hDAT function that accurately fits the main features of the experimental data. The model predicts that translocation of substrate occurs within milliseconds of substrate binding but that slow reorientation of the empty transporter is the rate-limiting factor for turnover. The model provides a framework for interpreting perturbations of hDAT activity.
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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.