Department of Biochemistry & Biophysics, UCSF School of Medicine, CA, USA; Departments of Neurology and Physiology, UCSF School of Medicine, CA, USA. Electronic address: https://twitter.com/Fei_UCSF.
Departments of Neurology and Physiology, UCSF School of Medicine, CA, USA. Electronic address: https://twitter.com/jcbrksn.
Curr Opin Struct Biol. 2022 Aug;75:102399. doi: 10.1016/j.sbi.2022.102399. Epub 2022 Jun 2.
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.
最初被鉴定为无机磷酸盐转运体的溶质载体 17(SLC17)家族蛋白具有多种生理作用。囊泡谷氨酸转运体(VGLUTs)将主要的兴奋性神经递质谷氨酸包装到突触小泡(SVs)中。相比之下,密切相关的唾液酸转运体唾液酸酶介导唾液酸从溶酶体向细胞质的相反方向流动。这两种蛋白以不同的方式与 H 电化学梯度驱动力偶联,大肠杆菌同源物 D-半乳糖酸盐转运体(DgoT)的高分辨率结构和最近的大鼠 VGLUT2 的结构开始提示涉及的机制以及底物特异性的基础。