GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters

Protein Sci. 2016 Mar;25(3):546-58. doi: 10.1002/pro.2858. Epub 2016 Jan 4.

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.

Keywords: GLUT; SGLT; SWEET; alternating access; glucose transporter; structural biology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Glucose / metabolism*
  • Glucose Transport Proteins, Facilitative / chemistry
  • Glucose Transport Proteins, Facilitative / metabolism*
  • Humans
  • Models, Molecular
  • Monosaccharide Transport Proteins / metabolism*
  • Protein Conformation
  • Sodium-Glucose Transport Proteins / chemistry
  • Sodium-Glucose Transport Proteins / metabolism*
  • Substrate Specificity

Substances

  • Glucose Transport Proteins, Facilitative
  • Monosaccharide Transport Proteins
  • Sodium-Glucose Transport Proteins
  • Glucose