GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters. (4th January 2016)

• Record Type: Journal Article
• Authors: Deng, Dong; Yan, Nieng
• Is Part Of: Protein science. Volume 25:Number 3(2016:Mar.)
• Page Start: 546
• Page End: 558
• Publication Date: 2016-01-04
• Subjects: glucose transporter -- GLUT -- SGLT -- SWEET -- alternating access -- structural biology; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2858
• Languages: English
• ISSNs: 0961-8368

Abstract

Abstract: Glucose is the primary fuel to life on earth. Cellular uptake of glucose is a fundamental process for metabolism, growth, and homeostasis. Three families of secondary glucose transporters have been identified in human, including the major facilitator superfamily glucose facilitators GLUTs, the sodium‐driven glucose symporters SGLTs, and the recently identified SWEETs. Structures of representative members or their prokaryotic homologs of all three families were obtained. This review focuses on the recent advances in the structural elucidation of the glucose transporters and the mechanistic insights derived from these structures, including the molecular basis for substrate recognition, alternating access, and stoichiometric coupling of co‐transport.