ArticleThe Journal of biological chemistry2012
Sequence determinants of GLUT1-mediated accelerated-exchange transport: analysis by homology-scanning mutagenesis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Insight into the Mechanism of d-Glucose Accelerated Exchange in GLUT1 from Molecular Dynamics Simulations.Biochemistry · 2025Article
- Quantifying glucose uptake at the single cell level with confocal microscopy reveals significant variability within and across individuals.Scientific reports · 2025Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Mechanistic Insights into Protein Stability and Self-aggregation in GLUT1 Genetic Variants Causing GLUT1-Deficiency Syndrome.The Journal of membrane biology · 2020Review
- Insulin-dependent, glucose transporter 1 mediated glucose uptake and tube formation in the human placental first trimester trophoblast cells.Molecular and cellular biochemistry · 2019Article
- 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
- Upregulation of Glucose Uptake and Hexokinase Activity of Primary Human CD4+ T Cells in Response to Infection with HIV-1.Viruses · 2018Article
- Kinetic Basis of Cis- and Trans-Allostery in GLUT1-Mediated Sugar Transport.The Journal of membrane biology · 2018Article
- A critique of the alternating access transporter model of uniport glucose transport.Biophysics reports · 2018Article
- Reconciling contradictory findings: Glucose transporter 1 (GLUT1) functions as an oligomer of allosteric, alternating access transporters.The Journal of biological chemistry · 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
- How does the chemical potential of the substrate drive a uniporter?Protein science : a publication of the Protein Society · 2016Article
- Uniporter substrate binding and transport: reformulating mechanistic questions.Biophysics reports · 2016Article
- Identification of residues important for substrate uptake in a glucose transporter from the filamentous fungus Trichoderma reesei.Scientific reports · 2015Article
- Critical Roles of Two Hydrophobic Residues within Human Glucose Transporter 9 (hSLC2A9) in Substrate Selectivity and Urate Transport.The Journal of biological chemistry · 2015Article
- Sequence determinants of GLUT1 oligomerization: analysis by homology-scanning mutagenesis.The Journal of biological chemistry · 2013Article
- Role of monosaccharide transport proteins in carbohydrate assimilation, distribution, metabolism, and homeostasis.Comprehensive Physiology · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The class 1 equilibrative glucose transporters GLUT1 and GLUT4 are structurally similar but catalyze distinct modes of transport. GLUT1 exhibits trans-acceleration, in which the presence of intracellular sugar stimulates the rate of unidirectional sugar uptake. GLUT4-mediated uptake is unaffected by intracellular sugar. Using homology-scanning mutagenesis in which domains of GLUT1 are substituted with equivalent domains from GLUT4 and vice versa, we show that GLUT1 transmembrane domain 6 is both necessary and sufficient for trans-acceleration. This region is not directly involved in GLUT1 binding of substrate or inhibitors. Rather, transmembrane domain 6 is part of two putative scaffold domains, which coordinate membrane-spanning amphipathic helices that form the sugar translocation pore. We propose that GLUT1 transmembrane domain 6 restrains import when intracellular sugar is absent by slowing transport-associated conformational changes.
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Registered trials
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.