Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.

Solute carriers form one of three major superfamilies of membrane transporters in humans, and include uniporters, exchangers and symporters. Following several decades of molecular characterisation, multiple solute carriers that form obligatory heteromers with unrelated subunits are emerging as a distinctive principle of membrane transporter assembly. Here we comprehensively review experimentally established heteromeric solute carriers: SLC3-SLC7 amino acid exchangers, SLC16 monocarboxylate/H symporters and basigin/embigin, SLC4A1 (AE1) and glycophorin A exchanger, SLC51 heteromer Ost α-Ost β uniporter, and SLC6 heteromeric symporters.

Novel Chemical Scaffolds to Inhibit the Neutral Amino Acid Transporter BAT1 (SLC6A19), a Potential Target to Treat Metabolic Diseases.

Lack of BAT1 (SLC6A19) partially protects mice against the onset of non-alcoholic steatohepatitis (NASH). To achieve a similar outcome through pharmacological treatment, we improved previously identified inhibitors of BAT1 by medicinal chemistry and identified second generation inhibitors by high through-put screening. Modified diarylmethine compounds inhibited BAT1 with IC values ranging from 8-90 μM.

Identification of novel inhibitors of the amino acid transporter B AT1 (SLC6A19), a potential target to induce protein restriction and to treat type 2 diabetes.

Background And Purpose: The neutral amino acid transporter B AT1 (SLC6A19) has recently been identified as a possible target to treat type 2 diabetes and related disorders. B AT1 mediates the Na -dependent uptake of all neutral amino acids. For surface expression and catalytic activity, B AT1 requires coexpression of collectrin (TMEM27).