ArticleThe Biochemical journal1998
Serine-294 and threonine-295 in the exofacial loop domain between helices 7 and 8 of glucose transporters (GLUT) are involved in the conformational alterations during the transport process.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 43 citations in OpenAlex.
- Liver Transcriptome Analysis Revealed the Physiological Response Mechanism of Red-Spotted Grouper (Animals : an open access journal from MDPI · 2026Article
- Human Glucose Transporters in Health and Selected Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- The role of salt bridge networks in the stability of the yeast hexose transporter 1.Biochimica et biophysica acta. General subjects · 2023Article
- Structure, function and regulation of mammalian glucose transporters of the SLC2 family.Pflugers Archiv : European journal of physiology · 2020Review
- Chemical biology probes of mammalian GLUT structure and function.The Biochemical journal · 2018Review
- Computational simulation and modeling of the blood-brain barrier pathology.Histochemistry and cell biology · 2018Review
- Article
- Functional architecture of MFS D-glucose transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- FGT-1 is the major glucose transporter in C. elegans and is central to aging pathways.The Biochemical journal · 2013Article
- Role of monosaccharide transport proteins in carbohydrate assimilation, distribution, metabolism, and homeostasis.Comprehensive Physiology · 2012Review
- Elucidation of the glucose transport pathway in glucose transporter 4 via steered molecular dynamics simulations.PloS one · 2011Article
- Transmembrane segments 1, 5, 7 and 8 are required for high-affinity glucose transport by Saccharomyces cerevisiae Hxt2 transporter.The Biochemical journal · 2003Article
- Activity and genomic organization of human glucose transporter 9 (GLUT9), a novel member of the family of sugar-transport facilitators predominantly expressed in brain and leucocytes.The Biochemical journal · 2000Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The role of a conserved polar motif (STS) in the exofacial loop between helices 7 and 8 of GLUT4 for transporter function was investigated by site-directed mutagenesis and expression of the constructs in COS-7 cells. Reconstituted glucose-transport activity, cytochalasin B binding and photolabelling with the exofacial label 2-N4-(1-azi-2,2,2-trifluoroethyl)benzoyl-1, 3-bis-(d-mannosyloxy)-2-propylamine (ATB-BMPA) were assayed in membranes from transfected cells and corrected for immunoreactivity of expressed transporters. Replacement of Ser-294 with Ala or Thr suppressed transport activity and cytochalasin B binding. ATB-BMPA photolabelling was normal in S294A mutants, and even increased in S294T mutants. Replacement of Thr-295 with Ala suppressed transport activity and cytochalasin B binding, whereas ATB-BMPA photolabelling was normal; substitution of Ser failed to alter the investigated parameters. Similarly, exchanging Ser-296 for Ala generated a normally functioning protein. The data suggest that Ser-294 and Thr-295 are involved in the conformational change in GLUT during the transport process, and that their substitution may arrest the transporter in an outward-facing conformation.
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