Diversity of function and mechanism in a family of organic anion transporters |
| |
| Institution: | 1. Department of Biochemistry & Biophysics, UCSF School of Medicine, CA, USA;2. Departments of Neurology and Physiology, UCSF School of Medicine, CA, USA;1. Center for Microbiology and Immunology, Lewis Katz School of Medicine, Temple University, Philadelphia, 19140, Pennsylvania, USA;2. Department of Bioengineering, Department of Chemistry & Biochemistry, California Nano Systems Institute, University of California, Los Angeles, Los Angeles, 90095, California, USA;1. Department of Bioengineering, University of California Riverside, 900 University Avenue, Riverside, CA, 52512, United States;2. Department of Chemistry, University of California Riverside, 900 University Avenue, Riverside, CA, 52512, United States;1. Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA;2. Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, 19107, USA;3. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA |
| |
| 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
