ArticleThe Journal of biological chemistry2008
Highly conserved asparagine 82 controls the interaction of Na+ with the sodium-coupled neutral amino acid transporter SNAT2.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Bacterial over-production of the functionally active human SLC38A2 (SNAT2) exploiting the mistic tag: a cheap and fast tool for testing ligands.Molecular biology reports · 2024Article
- Sodium-Dependent Neutral Amino Acid Transporter 2 Can Serve as a Tertiary Carrier for l-Type Amino Acid Transporter 1-Utilizing Prodrugs.Molecular pharmaceutics · 2023Article
- SNAT7 regulates mTORC1 via macropinocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Genetics Responses to Hypoxia and Reoxygenation Stress inAnimals : an open access journal from MDPI · 2021Article
- Review
- Metabolic Control over mTOR-Dependent Diapause-like State.Developmental cell · 2020Article
- Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state.Nature structural & molecular biology · 2018Article
- Effects of Sodium and Amino Acid Substrate Availability upon the Expression and Stability of the SNAT2 (SLC38A2) Amino Acid Transporter.Frontiers in pharmacology · 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
- Identification of a Disulfide Bridge in Sodium-Coupled Neutral Amino Acid Transporter 2(SNAT2) by Chemical Modification.PloS one · 2016Article
- SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1.Nature · 2015Article
- The SLC38 family of sodium-amino acid co-transporters.Pflugers Archiv : European journal of physiology · 2014Review
- The C-terminal domain of the neutral amino acid transporter SNAT2 regulates transport activity through voltage-dependent processes.The Biochemical journal · 2011Article
- Mutation of asparagine 76 in the center of glutamine transporter SNAT3 modulates substrate-induced conductances and Na+ binding.The Journal of biological chemistry · 2009Article
- A conserved Na(+) binding site of the sodium-coupled neutral amino acid transporter 2 (SNAT2).The Journal of biological chemistry · 2009Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The neutral amino acid transporter 2 (SNAT2), which belongs to the SLC38 family of solute transporters, couples the transport of amino acid to the cotransport of one Na(+) ion into the cell. Several polar amino acids are highly conserved within the SLC38 family. Here, we mutated three of these conserved amino acids, Asn(82) in the predicted transmembrane domain 1 (TMD1), Tyr(337) in TMD7, and Arg(374) in TMD8; and we studied the functional consequences of these modifications. The mutation of N82A virtually eliminated the alanine-induced transport current, as well as amino acid uptake by SNAT2. In contrast, the mutations Y337A and R374Q did not abolish amino acid transport. The K(m) of SNAT2 for its interaction with Na(+), K(Na(+)), was dramatically reduced by the N82A mutation, whereas the more conservative mutation N82S resulted in a K(Na(+)) that was in between SNAT2(N82A) and SNAT2(WT). These results were interpreted as a reduction of Na(+) affinity caused by the Asn(82) mutations, suggesting that these mutations interfere with the interaction of SNAT2 with the sodium ion. As a consequence of this dramatic reduction in Na(+) affinity, the apparent K(m) of SNAT2(N82A) for alanine was increased 27-fold compared with that of SNAT2(WT). Our results demonstrate a direct or indirect involvement of Asn(82) in Na(+) coordination by SNAT2. Therefore, we predict that TMD1 is crucial for the function of SLC38 transporters and that of related families.
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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.