How LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transporters

Aravind Penmatsa, Eric Gouaux

Research output: Contribution to journalArticle

59 Scopus citations

Abstract

Neurotransmitter transporters are ion-coupled symporters that drive the uptake of neurotransmitters from neural synapses. In the past decade, the structure of a bacterial amino acid transporter, leucine transporter (LeuT), has given valuable insights into the understanding of architecture and mechanism of mammalian neurotransmitter transporters. Different conformations of LeuT, including a substrate-free state, inward-open state, and competitive and non-competitive inhibitor-bound states, have revealed a mechanistic framework for the transport and transport inhibition of neurotransmitters. The current review integrates our understanding of the mechanistic and pharmacological properties of eukaryotic neurotransmitter transporters obtained through structural snapshots of LeuT.

Original languageEnglish (US)
Pages (from-to)863-869
Number of pages7
JournalJournal of Physiology
Volume592
Issue number5
DOIs
StatePublished - Mar 1 2014

ASJC Scopus subject areas

  • Physiology

Fingerprint Dive into the research topics of 'How LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transporters'. Together they form a unique fingerprint.

  • Cite this