Neurotransmitter transporters: Structure meets function

Paul J. Focke, Xiaoyu Wang, H. Peter Larsson

Research output: Contribution to journalReview articlepeer-review

38 Scopus citations


At synapses, sodium-coupled transporters remove released neurotransmitters, thereby recycling them and maintaining a low extracellular concentration of the neurotransmitter. The molecular mechanism underlying sodium-coupled neurotransmitter uptake is not completely understood. Several structures of homologs of human neurotransmitter transporters have been solved with X-ray crystallography. These crystal structures have spurred a plethora of computational and experimental work to elucidate the molecular mechanism underlying sodium-coupled transport. Here, we compare the structures of Glt Ph, a glutamate transporter homolog, and LeuT, a homolog of neurotransmitter transporters for the biogenic amines and inhibitory molecules GABA and glycine. We relate these structures to data obtained from experiments and computational simulations, to draw conclusions about the mechanism of uptake by sodium-coupled neurotransmitter transporters. Here, we propose how sodium and substrate binding is coupled and how binding of sodium and substrate opens and closes the gates in these transporters, thereby leading to an efficient coupled transport.

Original languageEnglish (US)
Pages (from-to)694-705
Number of pages12
Issue number5
StatePublished - May 7 2013

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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