Diversity of function and mechanism in a family of organic anion transporters. (August 2022)

• Record Type: Journal Article
• Authors: Li, Fei; Eriksen, Jacob; Finer-Moore, Janet; Stroud, Robert M.; Edwards, Robert H.
• Is Part Of: Current opinion in structural biology. Volume 75(2022)
• Publication Date: 2022-08
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2022.102399
• Languages: English
• ISSNs: 0959-440X

Abstract

Abstract: Originally identified as transporters for inorganic phosphate, solute carrier 17 (SLC17) family proteins subserve diverse physiological roles. The vesicular glutamate transporters (VGLUTs) package the principal excitatory neurotransmitter glutamate into synaptic vesicles (SVs). In contrast, the closely related sialic acid transporter sialin mediates the flux of sialic acid in the opposite direction, from lysosomes to the cytoplasm. The two proteins couple in different ways to the H + electrochemical gradient driving force, and high-resolution structures of the Escherichia coli homolog d -galactonate transporter (DgoT) and more recently rat VGLUT2 now begin to suggest the mechanisms involved as well as the basis for substrate specificity. Highlights: SLC17 family proteins transport organic anions using diverse mechanisms. Vesicular glutamate transporters are allosterically regulated by pH. E. coli homologue DgoT cotransports d -galactonate with H + . Structures reveal the basis for substrate recognition by DgoT and VGLUT2.