ArticleNature communications2022
Cryo-EM structure of human glucose transporter GLUT4.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 75 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
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- Technology-enabled insights into SLC transporters in MAFLD: redefining the multi-hit pathogenesis and therapeutic landscape.Acta pharmacologica Sinica · 2026Review
- High-resolution cryo-EM structures of small protein-ligand complexes near the theoretical size limit.Nature communications · 2026Article
- Canonical and Alternative Pathways (Insulin and Exercise) of GLUT4 Synthesis, Signaling, Intracellular Clustering, and Recruitment to the Plasma Membrane.International journal of molecular sciences · 2026Review
- Vitamin KJournal of animal science and biotechnology · 2026Article
- A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026Article
- Efficient Sampling of Short Protein Trajectories with Conditional Diffusion Models.Journal of chemical theory and computation · 2026Article
- Research progress on TMEM proteins in cancer progression and chemoresistance (Review).International journal of molecular medicine · 2025Review
- Integrated Transcriptomic and Metabolomic Analysis RevealsFoods (Basel, Switzerland) · 2025Article
- Eggplant (International journal of molecular sciences · 2025Article
- Advanced optical microscopy methods forBiophysical reviews · 2025Review
- Matrix metalloproteinase-2 as a novel regulator of glucose utilization by adipocytes.Scientific reports · 2025Article
- Adaptive gradient scaling: integrating Adam and landscape modification for protein structure prediction.BMC bioinformatics · 2025Article
- Nanodiscs remain indispensable for Cryo-EM studies of membrane proteins.Current opinion in structural biology · 2025Review
- Intracellular calcium channels: Potential targets for type 2 diabetes mellitus?World journal of diabetes · 2025Review
- Effect of Galactooligosaccharide on PPARs/PI3K/Akt Pathway and Gut Microbiota in High-Fat and High-Sugar Diet Combined with STZ-Induced GDM Rat Model.Probiotics and antimicrobial proteins · 2025Article
- Structural basis of disease mutation and substrate recognition by the human SLC2A9 transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Advances in cryo-electron microscopy (cryoEM) for structure-based drug discovery.Expert opinion on drug discovery · 2025Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GLUT4 is the primary glucose transporter in adipose and skeletal muscle tissues. Its cellular trafficking is regulated by insulin signaling. Failed or reduced plasma membrane localization of GLUT4 is associated with diabetes. Here, we report the cryo-EM structures of human GLUT4 bound to a small molecule inhibitor cytochalasin B (CCB) at resolutions of 3.3 Å in both detergent micelles and lipid nanodiscs. CCB-bound GLUT4 exhibits an inward-open conformation. Despite the nearly identical conformation of the transmembrane domain to GLUT1, the cryo-EM structure reveals an extracellular glycosylation site and an intracellular helix that is invisible in the crystal structure of GLUT1. The structural study presented here lays the foundation for further mechanistic investigation of the modulation of GLUT4 trafficking. Our methods for cryo-EM analysis of GLUT4 will also facilitate structural determination of many other small size solute carriers.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.