ArticleThe Journal of biological chemistry2009
Mutation of asparagine 76 in the center of glutamine transporter SNAT3 modulates substrate-induced conductances and Na+ binding.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Sequence analysis and function of mosquito aeCCC2 and Drosophila Ncc83 orthologs.Insect biochemistry and molecular biology · 2022Article
- Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state.Nature structural & molecular biology · 2018Article
- Rapid sensing of l-leucine by human and murine hypothalamic neurons: Neurochemical and mechanistic insights.Molecular metabolism · 2018Article
- SNAT7 is the primary lysosomal glutamine exporter required for extracellular protein-dependent growth of cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The SLC38 family of sodium-amino acid co-transporters.Pflugers Archiv : European journal of physiology · 2014Review
- Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.The Journal of biological chemistry · 2011Article
- The C-terminal domain of the neutral amino acid transporter SNAT2 regulates transport activity through voltage-dependent processes.The Biochemical journal · 2011Article
- Astrocyte glutamine synthetase: importance in hyperammonemic syndromes and potential target for therapy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2010Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glutamine transporter SLC38A3 (SNAT3) plays an important role in the release of glutamine from brain astrocytes and the uptake of glutamine into hepatocytes. It is related to the vesicular GABA (gamma-aminobutyric acid) transporter and the SLC36 family of proton-amino acid cotransporters. The transporter carries out electroneutral Na+-glutamine cotransport-H+ antiport. In addition, substrate-induced uncoupled cation currents are observed. Mutation of asparagine 76 to glutamine or histidine in predicted transmembrane helix 1 abolished all substrate-induced currents. Mutation of asparagine 76 to aspartate rendered the transporter Na+-independent and resulted in a gain of a large substrate-induced chloride conductance in the absence of Na+. Thus, a single residue is critical for coupled and uncoupled ion flows in the glutamine transporter SNAT3. Homology modeling of SNAT3 along the structure of the related benzyl-hydantoin permease from Microbacterium liquefaciens reveals that Asn-76 is likely to be located in the center of the membrane close to the translocation pore and forms part of the predicted Na+ -binding site.
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