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Article

An N-terminal threonine mutation produces an efflux-favorable, sodium-primed conformation of the human dopamine transporter.

Molecular pharmacology - 1 Jul 2014

Fraser Rheaclare, Chen Yongyue, Guptaroy Bipasha, Luderman Kathryn D, Stokes Stephanie L, Beg Asim, DeFelice Louis J, Gnegy Margaret E

Abstract excerpt

The dopamine transporter (DAT) reversibly transports dopamine (DA) through a series of conformational transitions. Alanine (T62A) or aspartate (T62D) mutagenesis of Thr62 revealed T62D-human (h)DAT partitions in a predominately efflux-preferring conformation. Compared with wild-type (WT), T62D-hDAT exhibits reduced [(3)H]DA uptake and enhanced baseline DA efflux, whereas T62A-hDAT and WT-hDAT function in an...

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Identifiers

PMID: 24753048
DOI: 10.1124/mol.114.091926
PMCID: PMC4053999

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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