ArticleNeurochemical research2016
The Split Personality of Glutamate Transporters: A Chloride Channel and a Transporter.
Article in Neurochemical research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6.Nature communications · 2023Article
- Microscopic Characterization of the Chloride Permeation Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).ACS chemical neuroscience · 2022Article
- Review
- ATP Synthase KFunction (Oxford, England) · 2022Article
- Heterologous Expression ofInsects · 2019Article
- Aluminum-Activated Malate Transporters Can Facilitate GABA Transport.The Plant cell · 2018Article
- Cystic fibrosis transmembrane conductance regulator (CFTR): Making an ion channel out of an active transporter structure.Channels (Austin, Tex.) · 2018Review
- Channel surfing uncovers a dual-use transporter.The EMBO journal · 2017Article
- Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters.eLife · 2017Article
- Disruption of an EAAT-Mediated Chloride Channel in a Drosophila Model of Ataxia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Tuning the ion selectivity of glutamate transporter-associated uncoupled conductances.The Journal of general physiology · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transporters and ion channels are conventionally categorised into distinct classes of membrane proteins. However, some membrane proteins have a split personality and can function as both transporters and ion channels. The excitatory amino acid transporters (EAATs) in particular, function as both glutamate transporters and chloride (Cl(-)) channels. The EAATs couple the transport of glutamate to the co-transport of three Na(+) ions and one H(+) ion into the cell, and the counter-transport of one K(+) ion out of the cell. The EAAT Cl(-) channel is activated by the binding of glutamate and Na(+), but is thermodynamically uncoupled from glutamate transport and involves molecular determinants distinct from those responsible for glutamate transport. Several crystal structures of an EAAT archaeal homologue, GltPh, at different stages of the transport cycle, alongside numerous functional studies and molecular dynamics simulations, have provided extensive insights into the mechanism of substrate transport via these transporters. However, the molecular determinants involved in Cl(-) permeation, and the mechanism by which this channel is activated are not entirely understood. Here we will discuss what is currently known about the molecular determinants involved in EAAT-mediated Cl(-) permeation and the mechanisms that underlie their split personality.
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Registered trials
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