ArticleThe Journal of biological chemistry2013
Sequence determinants of GLUT1 oligomerization: analysis by homology-scanning mutagenesis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Glucose Transporters: Structure, Trafficking, Physiology, and Disease Relevance.Current issues in molecular biology · 2026Review
- Insight into the Mechanism of d-Glucose Accelerated Exchange in GLUT1 from Molecular Dynamics Simulations.Biochemistry · 2025Article
- Sphingosine-1-phosphate suppresses GLUT activity through PP2A and counteracts hyperglycemia in diabetic red blood cells.Nature communications · 2023Article
- GLUT3 regulates alternative macrophage signaling through a glucose transport-independent role.The Journal of clinical investigation · 2023Article
- Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family.Life science alliance · 2021Article
- Structure, function and regulation of mammalian glucose transporters of the SLC2 family.Pflugers Archiv : European journal of physiology · 2020Review
- Mechanistic Insights into Protein Stability and Self-aggregation in GLUT1 Genetic Variants Causing GLUT1-Deficiency Syndrome.The Journal of membrane biology · 2020Review
- Transporter oligomerisation: roles in structure and function.Biochemical Society transactions · 2019Review
- Red wine and green tea flavonoids areThe Journal of biological chemistry · 2018Article
- Chemical biology probes of mammalian GLUT structure and function.The Biochemical journal · 2018Review
- Intestinal Absorption of Fructose.Annual review of nutrition · 2018Review
- Kinetic Basis of Cis- and Trans-Allostery in GLUT1-Mediated Sugar Transport.The Journal of membrane biology · 2018Article
- Reconciling contradictory findings: Glucose transporter 1 (GLUT1) functions as an oligomer of allosteric, alternating access transporters.The Journal of biological chemistry · 2017Article
- Metabolic and redox signaling in the retina.Cellular and molecular life sciences : CMLS · 2017Review
- Current carried by the Slc26 family member prestin does not flow through the transporter pathway.Scientific reports · 2017Article
- Membrane Phase-Dependent Occlusion of Intramolecular GLUT1 Cavities Demonstrated by Simulations.Biophysical journal · 2017Article
- WZB117 (2-Fluoro-6-(m-hydroxybenzoyloxy) Phenyl m-Hydroxybenzoate) Inhibits GLUT1-mediated Sugar Transport by Binding Reversibly at the Exofacial Sugar Binding Site.The Journal of biological chemistry · 2016Article
- Determination of GLUT1 Oligomerization Parameters using Bioluminescent Förster Resonance Energy Transfer.Scientific reports · 2016Article
- Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.Nature communications · 2016Article
- Clathrin binding by the adaptor Ent5 promotes late stages of clathrin coat maturation.Molecular biology of the cell · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The human blood-brain barrier glucose transport protein (GLUT1) forms homodimers and homotetramers in detergent micelles and in cell membranes, where the GLUT1 oligomeric state determines GLUT1 transport behavior. GLUT1 and the neuronal glucose transporter GLUT3 do not form heterocomplexes in human embryonic kidney 293 (HEK293) cells as judged by co-immunoprecipitation assays. Using homology-scanning mutagenesis in which GLUT1 domains are substituted with equivalent GLUT3 domains and vice versa, we show that GLUT1 transmembrane helix 9 (TM9) is necessary for optimal association of GLUT1-GLUT3 chimeras with parental GLUT1 in HEK cells. GLUT1 TMs 2, 5, 8, and 11 also contribute to a less abundant heterocomplex. Cell surface GLUT1 and GLUT3 containing GLUT1 TM9 are 4-fold more catalytically active than GLUT3 and GLUT1 containing GLUT3 TM9. GLUT1 and GLUT3 display allosteric transport behavior. Size exclusion chromatography of detergent solubilized, purified GLUT1 resolves GLUT1/lipid/detergent micelles as 6- and 10-nm Stokes radius particles, which correspond to GLUT1 dimers and tetramers, respectively. Studies with GLUTs expressed in and solubilized from HEK cells show that HEK cell GLUT1 resolves as 6- and 10-nm Stokes radius particles, whereas GLUT3 resolves as a 6-nm particle. Substitution of GLUT3 TM9 with GLUT1 TM9 causes chimeric GLUT3 to resolve as 6- and 10-nm Stokes radius particles. Substitution of GLUT1 TM9 with GLUT3 TM9 causes chimeric GLUT1 to resolve as a mixture of 6- and 4-nm particles. We discuss these findings in the context of determinants of GLUT oligomeric structure and transport function.
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