Excitatory amino acid transporter 3 (EAAT3), is a protein that in humans is encoded by the SLC1A1 gene.[5][6]
SLC1A1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | SLC1A1, EAAC1, EAAT3, SCZD18, DCBXA, solute carrier family 1 member 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 133550 MGI: 105083 HomoloGene: 20881 GeneCards: SLC1A1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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EAAT3 is expressed on the plasma membrane of neurons, specifically on the dendrites and axon terminals.[7]
Excitatory amino acid transporter 3 is a member of the high-affinity glutamate transporters which plays an essential role in transporting glutamate across plasma membranes in neurons. In the brain, excitatory amino acid transporters are crucial in terminating the postsynaptic action of the neurotransmitter glutamate, and in maintaining extracellular glutamate concentrations below neurotoxic levels. EAAT3 also transports aspartate, and mutations in this gene are thought to cause dicarboxylic aminoaciduria, also known as glutamate-aspartate transport defect.[6] EAAT3 is also the major route of neuronal cysteine uptake. Cysteine is a component of the major antioxidant glutathione, and mice lacking EAAT3 exhibit reduced levels of glutathione in neurons, increased oxidative stress, and age-dependent loss of neurons, especially neurons of the substantia nigra. A meta-analysis identified a small but significant association between a polymorphism of the gene SLC1A1 and Obsessive-Compulsive Disorder.[8]
In general, EAATs 1 and 2 are found predominantly in astrocytes, EAAT3 in neurons, EAAT4 in Purkinje cells, and EAAT5 expression is restricted to the retina (Danbolt, 2001). The dependence of EAAT3 internalization on the DAT also suggests that the two transporters might be internalized together. We found that EAAT3 and DAT are expressed in the same cells, as well as in axons and dendrites. However, the subcellular co-localization of the two neurotransmitter transporters remains to be established definitively by high resolution electron microscopy.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.