Abstract
In brain cells, glutamine transporters are vital to monitor and control the levels of glutamate andGABA. There are 11 members of theSLC38 family of amino acid transporters of which eight have been functionally characterized. Here, we report the first histological and functional characterization of the previously orphan member,SLC38A10. We used pairwise global sequence alignments to determine the sequence identity between theSLC38 family members.SLC38A10 was found to share 20–25% transmembrane sequence identity with several family members, and was predicted to have 11 transmembrane helices.SLC38A10 immunostaining was abundant in mouse brain using a custom‐made anti‐SLC38A10 antibody and colocalization ofSLC38A10 immunoreactivity with markers for neurons and astrocytes was detected. UsingXenopus laevisoocytes overexpressingSLC38A10, we show thatSLC38A10 mediates bidirectional transport ofl‐glutamine,l‐alanine,l‐glutamate, andd‐aspartate, and efflux ofl‐serine. This profile mostly resembles system A members of theSLC38 family. In conclusion, the bidirectional transport of glutamine, glutamate, and aspartate bySLC38A10, and the immunostaining detected in neurons and astrocytes, suggest thatSLC38A10 plays a role in pathways involved in neurotransmission.
Funding Information
  • Svenska Forskningsrådet Formas
  • Hjärnfonden
  • Svenska Sällskapet för Medicinsk Forskning

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