ArticleScientific reports2017
Establishing a yeast-based screening system for discovery of human GLUT5 inhibitors and activators.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- GB5, a synergistic phytotherapy for type 2 diabetes mellitus management: an integrated polyherbal approach from phytochemical profiling to network pharmacology.BMC complementary medicine and therapies · 2025Article
- Role and mechanism of circ_001024 endogenous competition for miR-145-3p targeting to regulate GLUT5 in RCC.BMC cancer · 2025Article
- Functional analysis of Saccharomyces cerevisiae FLO genes through optogenetic control.FEMS yeast research · 2025Article
- Regulation of Fructose Metabolism in Nonalcoholic Fatty Liver Disease.Biomolecules · 2024Review
- GLUT5: structure, functions, diseases and potential applications.Acta biochimica et biophysica Sinica · 2023Review
- Discrimination of GLUTs by Fructose Isomers Enables Simultaneous Screening of GLUT5 and GLUT2 Activity in Live Cells.ACS chemical biology · 2023Article
- A Fluorescence-Based Assay to Probe Inhibitory Effect of Fructose Mimics on GLUT5 Transport in Breast Cancer Cells.ACS bio & med chem Au · 2023Article
- Heterologous (Over) Expression of Human SoLute Carrier (SLC) in Yeast: A Well-Recognized Tool for Human Transporter Function/Structure Studies.Life (Basel, Switzerland) · 2022Review
- Gene variants of the SLC2A5 gene encoding GLUT5, the major fructose transporter, do not contribute to clinical presentation of acquired fructose malabsorption.BMC gastroenterology · 2022Article
- GLUT3 inhibitor discovery through in silico ligand screening and in vivo validation in eukaryotic expression systems.Scientific reports · 2022Article
- Identification of new GLUT2-selective inhibitors through in silico ligand screening and validation in eukaryotic expression systems.Scientific reports · 2021Article
- An Overview of Cell-Based Assay Platforms for the Solute Carrier Family of Transporters.Frontiers in pharmacology · 2021Review
- Permuted 2,4-thiazolidinedione (TZD) analogs as GLUT inhibitors and their in-vitro evaluation in leukemic cells.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2020Article
- Structure guided design and synthesis of furyl thiazolidinedione derivatives as inhibitors of GLUT 1 and GLUT 4, and evaluation of their anti-leukemic potential.European journal of medicinal chemistry · 2020Article
- Discovery of novel N-substituted thiazolidinediones (TZDs) as HDAC8 inhibitors: in-silico studies, synthesis, and biological evaluation.Bioorganic chemistry · 2020Article
- Functional Expression of the Human Glucose Transporters GLUT2 and GLUT3 in Yeast Offers Novel Screening Systems for GLUT-Targeting Drugs.Frontiers in molecular biosciences · 2020Article
- Review
- Intestinal Saturated Long-Chain Fatty Acid, Glucose and Fructose Transporters and Their Inhibition by Natural Plant Extracts in Caco-2 Cells.Molecules (Basel, Switzerland) · 2018Review
- Ligand Screening Systems for Human Glucose Transporters as Tools in Drug Discovery.Frontiers in chemistry · 2018Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Human GLUT5 is a fructose-specific transporter in the glucose transporter family (GLUT, SLC2 gene family). Its substrate-specificity and tissue-specific expression make it a promising target for treatment of diabetes, metabolic syndrome and cancer, but few GLUT5 inhibitors are known. To identify and characterize potential GLUT5 ligands, we developed a whole-cell system based on a yeast strain deficient in fructose uptake, in which GLUT5 transport activity is associated with cell growth in fructose-based media or assayed by fructose uptake in whole cells. The former method is convenient for high-throughput screening of potential GLUT5 inhibitors and activators, while the latter enables detailed kinetic characterization of identified GLUT5 ligands. We show that functional expression of GLUT5 in yeast requires mutations at specific positions of the transporter sequence. The mutated proteins exhibit kinetic properties similar to the wild-type transporter and are inhibited by established GLUT5 inhibitors N-[4-(methylsulfonyl)-2-nitrophenyl]-1,3-benzodioxol-5-amine (MSNBA) and (-)-epicatechin-gallate (ECG). Thus, this system has the potential to greatly accelerate the discovery of compounds that modulate the fructose transport activity of GLUT5.
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