Cysteine Transport through Excitatory Amino Acid Transporter 3 (EAAT3)
Open accessAbstract
Excitatory amino acid transporters (EAATs) limit glutamatergic signaling and maintain extracellular glutamate concentrations below neurotoxic levels. Of the five known EAAT isoforms (EAATs 1-5), only the neuronal isoform, EAAT3 (EAAC1), can efficiently transport the uncharged amino acid L-cysteine. EAAT3-mediated cysteine transport has been proposed to be a primary mechanism used by neurons to obtain cysteine for the synthesis of glutathione, a key molecule in preventing oxidative stress and neuronal toxicity. The molecular mechanisms underlying the selective transport of cysteine by EAAT3 have not been elucidated. Here we propose that the transport of cysteine through EAAT3 requires formation of the thiolate form of cysteine in the binding site. Using Xenopus oocytes and HEK293 cells expressing EAAT2 and EAAT3, we assessed the transport kinetics of different substrates and measured transporter-associated currents electrophysiologically. Our results show that L-selenocysteine, a cysteine analog that forms a negatively-charged selenolate ion at physiological pH, is efficiently transported by EAATs 1-3 and has a much higher apparent affinity for transport when compared to cysteine. Using a membrane tethered GFP variant to monitor intracellular pH changes associated with transport activity, we observed that transport of either L-glutamate or L-selenocysteine by EAAT3 decreased intracellular pH, whereas transport of cysteine resulted in cytoplasmic alkalinization. No change in pH was observed when cysteine was applied to cells expressing EAAT2, which displays negligible transport of cysteine. Under conditions that favor release of intracellular substrates through EAAT3 we observed release of labeled intracellular glutamate but did not detect cysteine release. Our results support a model whereby cysteine transport through EAAT3 is facilitated through cysteine de-protonation and that once inside, the thiolate is rapidly re-protonated. Moreover, these findings suggest that cysteine transport is predominantly unidirectional and that reverse transport does not contribute to depletion of intracellular cysteine pools.
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Membrane transport of organo-Se species SeMet and SeCys occurs via shared transporters in animal and human cells.
“The membrane-transport of organo-Se species SeMet and SeCys has been investigated in animal and human cells and also occurs via shared transporters [188], i.e., methionine [189] and cysteine [190] transporters.”
From Selenium Cycling Across Soil-Plant-Atmosphere Interfaces: A Critical Review (2015) · cites this paper as [190]
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- Authors
- Watts, S. D., Torres-Salazar, D., Divito, C. B., & Amara, S. G.
- Affiliations
- University of Pittsburgh (US)
- National Institutes of Health (US)
- Corresponding author
- Amara, Susan G.
- ORCID
- Amara, Susan G.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2014-10-02
- Volume
- 9
- Issue
- 10
- Pages
- e109245
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4183567
- OpenAlex
- W1964948381
- Cited by
- 55
- References
- 41
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 6 · 2023: 3 · 2022: 6 · 2021: 4 · 2020: 6 · 2019: 8 · 2018: 5 · 2017: 6 · 2016: 2 · 2015: 3
- FWCI
- 1.63
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- Europe PMC (PubMed Central) (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- D-Scholarship@Pitt (University of Pittsburgh) (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- American Heart Association
- Oregon Health and Science University
- National Institutes of Health
- National Institute of Mental Health (R01MH080726, MH080726)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- EAAT3, EAAC1, cysteine transport, glutamate transporters, glutamate uptake, thiolate, glutathione synthesis, intracellular pH, unidirectional transport, glutamate release, GLT-1
- MeSH terms
- Animals, Cysteine, Humans, Hydrogen-Ion Concentration, Oocytes, Xenopus, Selenocysteine, Glutamic Acid, Excitatory Amino Acid Transporter 2, Excitatory Amino Acid Transporter 3, HEK293 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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