ArticleThe Journal of general physiology2001
Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1.
Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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85 citing papers in PubMed, 127 citations in OpenAlex.
- The Charge of the Substrate Determines Sodium-Coupling Stoichiometry of the Amino Acid Transporter SLC6A14.Biochemistry · 2025Article
- Structural basis of excitatory amino acid transporter 3 substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of the excitatory amino acid transporter 3 substrate recognition.bioRxiv : the preprint server for biology · 2024Article
- Glutamate transporters are involved in direct inhibitory synaptic transmission in the vertebrate retina.Open biology · 2024Article
- Symport and antiport mechanisms of human glutamate transporters.Nature communications · 2023Article
- Article
- Functional and Kinetic Comparison of Alanine Cysteine Serine Transporters ASCT1 and ASCT2.Biomolecules · 2022Article
- Pre-Steady-State Kinetics and Reverse Transport in Rat Glutamate Transporter EAAC1 with an Immobilized Transport Domain.Neurochemical research · 2022Article
- Cryo-EM structures of excitatory amino acid transporter 3 visualize coupled substrate, sodium, and proton binding and transport.Science advances · 2021Article
- Pre-steady-state Kinetic Analysis of Amino Acid Transporter SLC6A14 Reveals Rapid Turnover Rate and Substrate Translocation.Frontiers in physiology · 2021Article
- Article
- Regulation of Glutamate, GABA and Dopamine Transporter Uptake, Surface Mobility and Expression.Frontiers in cellular neuroscience · 2021Review
- Mechanism and potential sites of potassium interaction with glutamate transporters.The Journal of general physiology · 2020Article
- A KThe Journal of biological chemistry · 2019Article
- Novel alanine serine cysteine transporter 2 (ASCT2) inhibitors based on sulfonamide and sulfonic acid ester scaffolds.The Journal of general physiology · 2019Article
- Article
- Both reentrant loops of the sodium-coupled glutamate transporters contain molecular determinants of cation selectivity.The Journal of biological chemistry · 2018Article
- Carriers, exchangers, and cotransporters in the first 100 years of theThe Journal of general physiology · 2018Review
- Impaired KScientific reports · 2017Article
- Gating Charge Calculations by Computational Electrophysiology Simulations.Biophysical journal · 2017Article
25 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrogenic glutamate transport by the excitatory amino acid carrier 1 (EAAC1) is associated with multiple charge movements across the membrane that take place on time scales ranging from microseconds to milliseconds. The molecular nature of these charge movements is poorly understood at present and, therefore, was studied in this report in detail by using the technique of laser-pulse photolysis of caged glutamate providing a 100-micros time resolution. In the inward transport mode, the deactivation of the transient component of the glutamate-induced coupled transport current exhibits two exponential components. Similar results were obtained when restricting EAAC1 to Na(+) translocation steps by removing potassium, thus, demonstrating (1) that substrate translocation of EAAC1 is coupled to inward movement of positive charge and, therefore, electrogenic; and (2) the existence of at least two distinct intermediates in the Na(+)-binding and glutamate translocation limb of the EAAC1 transport cycle. Together with the determination of the sodium ion concentration and voltage dependence of the two-exponential charge movement and of the steady-state EAAC1 properties, we developed a kinetic model that is based on sequential binding of Na(+) and glutamate to their extracellular binding sites on EAAC1 explaining our results. In this model, at least one Na(+) ion and thereafter glutamate rapidly bind to the transporter initiating a slower, electroneutral structural change that makes EAAC1 competent for further, voltage-dependent binding of additional sodium ion(s). Once the fully loaded EAAC1 complex is formed, it can undergo a much slower, electrogenic translocation reaction to expose the substrate and ion binding sites to the cytoplasm.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.