ArticleThe Journal of biological chemistry2013
Mutating a conserved proline residue within the trimerization domain modifies Na+ binding to excitatory amino acid transporters and associated conformational changes.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 22 citations in OpenAlex.
- Overactive EAAT1 ClActa neuropathologica communications · 2026Article
- Multimodal dynamics control activity of a glial glutamate transporter.bioRxiv : the preprint server for biology · 2026Article
- Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6.Nature communications · 2023Article
- Article
- Ataxia-linked SLC1A3 mutations alter EAAT1 chloride channel activity and glial regulation of CNS function.The Journal of clinical investigation · 2022Article
- Microscopic Characterization of the Chloride Permeation Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).ACS chemical neuroscience · 2022Article
- Molecular Basis of Coupled Transport and Anion Conduction in Excitatory Amino Acid Transporters.Neurochemical research · 2022Review
- Article
- Amino Acid Transporters and Exchangers from the SLC1A Family: Structure, Mechanism and Roles in Physiology and Cancer.Neurochemical research · 2020Review
- SLC1A3 C3590T but not BDNF G196A is a predisposition factor for stress as well as depression, in an adolescent eastern Indian population.BMC medical genetics · 2020Article
- Increased glutamate transporter-associated anion currents cause glial apoptosis in episodic ataxia 6.Brain communications · 2020Article
- Impaired KScientific reports · 2017Article
- De Novo Mutations in YWHAG Cause Early-Onset Epilepsy.American journal of human genetics · 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
- Functional properties of the retinal glutamate transporters GLT-1c and EAAT5.The Journal of biological chemistry · 2014Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Excitatory amino acid transporters (EAATs) are crucial for glutamate homeostasis in the mammalian central nervous system. They are not only secondary active glutamate transporters but also function as anion channels, and different EAATs vary considerably in glutamate transport rates and associated anion current amplitudes. A naturally occurring mutation, which was identified in a patient with episodic ataxia type 6 and that predicts the substitution of a highly conserved proline at position 290 by arginine (P290R), was recently shown to reduce glutamate uptake and to increase anion conduction by hEAAT1. We here used voltage clamp fluorometry to define how the homologous P259R mutation modifies the functional properties of hEAAT3. P259R inverts the voltage dependence, changes the sodium dependence, and alters the time dependence of hEAAT3 fluorescence signals. Kinetic analysis of fluorescence signals indicate that P259R decelerates a conformational change associated with sodium binding to the glutamate-free mutant transporters. This alteration in the glutamate uptake cycle accounts for the experimentally observed changes in glutamate transport and anion conduction by P259R hEAAT3.
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