ArticleThe Journal of biological chemistry2011
Hetero-oligomerization of neuronal glutamate transporters.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Expanding the genetic and phenotypic relevance of CLCN4 variants in neurodevelopmental condition: 13 new patients.Journal of neurology · 2024Article
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- Molecular Basis of Coupled Transport and Anion Conduction in Excitatory Amino Acid Transporters.Neurochemical research · 2022Review
- Functional Characterization ofFrontiers in molecular neuroscience · 2022Article
- Cellular Physiology and Pathophysiology of EAAT Anion Channels.Frontiers in cellular neuroscience · 2021Review
- Neurobiology, Functions, and Relevance of Excitatory Amino Acid Transporters (EAATs) to Treatment of Refractory Epilepsy.CNS drugs · 2020Review
- Excitatory Amino Acid Transporters in Physiology and Disorders of the Central Nervous System.International journal of molecular sciences · 2019Review
- Preferential association with ClC-3 permits sorting of ClC-4 into endosomal compartments.The Journal of biological chemistry · 2017Article
- Impaired KScientific reports · 2017Article
- Reduced Membrane Insertion of CLC-K by V33L Barttin Results in Loss of Hearing, but Leaves Kidney Function Intact.Frontiers in physiology · 2017Article
- The importance of the excitatory amino acid transporter 3 (EAAT3).Neurochemistry international · 2016Review
- Carboxyl-terminal Truncations of ClC-Kb Abolish Channel Activation by Barttin Via Modified Common Gating and Trafficking.The Journal of biological chemistry · 2015Article
- Characterization of a Novel Mutation in SLC1A1 Associated with Schizophrenia.Molecular neuropsychiatry · 2015Article
- Glutamate transporter EAAT2: regulation, function, and potential as a therapeutic target for neurological and psychiatric disease.Cellular and molecular life sciences : CMLS · 2015Review
- Tryptophan Scanning Mutagenesis Identifies the Molecular Determinants of Distinct Barttin Functions.The Journal of biological chemistry · 2015Article
- Human CLC-K Channels Require Palmitoylation of Their Accessory Subunit Barttin to Be Functional.The Journal of biological chemistry · 2015Article
- Differential regulation of two isoforms of the glial glutamate transporter EAAT2 by DLG1 and CaMKII.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Changes in the expression of the glutamate transporter EAAT3/EAAC1 in health and disease.Cellular and molecular life sciences : CMLS · 2014Review
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Excitatory amino acid transporters (EAATs) mediate the uptake of glutamate into neuronal and glial cells of the mammalian central nervous system. Two transporters expressed primarily in glia, EAAT1 and EAAT2, are crucial for glutamate homeostasis in the adult mammalian brain. Three neuronal transporters (EAAT3, EAAT4, and EAAT5) appear to have additional functions in regulating and processing cellular excitability. EAATs are assembled as trimers, and the existence of multiple isoforms raises the question of whether certain isoforms can form hetero-oligomers. Co-expression and pulldown experiments of various glutamate transporters showed that EAAT3 and EAAT4, but neither EAAT1 and EAAT2, nor EAAT2 and EAAT3 are capable of co-assembling into heterotrimers. To study the functional consequences of hetero-oligomerization, we co-expressed EAAT3 and the serine-dependent mutant R501C EAAT4 in HEK293 cells and Xenopus laevis oocytes and studied glutamate/serine transport and anion conduction using electrophysiological methods. Individual subunits transport glutamate independently of each other. Apparent substrate affinities are not affected by hetero-oligomerization. However, polarized localization in Madin-Darby canine kidney cells was different for homo- and hetero-oligomers. EAAT3 inserts exclusively into apical membranes of Madin-Darby canine kidney cells when expressed alone. Co-expression with EAAT4 results in additional appearance of basolateral EAAT3. Our results demonstrate the existence of heterotrimeric glutamate transporters and provide novel information about the physiological impact of EAAT oligomerization.
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Registered trials
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.