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Glucose transporters in the 21st Century
Open accessAbstract
The ability to take up and metabolize glucose at the cellular level is a property shared by the vast majority of existing organisms. Most mammalian cells import glucose by a process of facilitative diffusion mediated by members of the Glut (SLC2A) family of membrane transport proteins. Fourteen Glut proteins are expressed in the human and they include transporters for substrates other than glucose, including fructose, myoinositol, and urate. The primary physiological substrates for at least half of the 14 Glut proteins are either uncertain or unknown. The well-established glucose transporter isoforms, Gluts 1–4, are known to have distinct regulatory and/or kinetic properties that reflect their specific roles in cellular and whole body glucose homeostasis. Separate review articles on many of the Glut proteins have recently appeared in this journal. Here, we provide a very brief summary of the known properties of the 14 Glut proteins and suggest some avenues of future investigation in this area.
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“In particular, insulin facilitates the translocation of GLUT1, GLUT3 and GLUT4 from intracellular pools to the cell membrane to amplify the glucose uptake in adipocytes and muscle cells, while GCs antagonize this process by translocating GLUTs from the cell membrane back to intracellular compartments (26, 27).”
From The progression of secondary diabetes: A review of modeling studies (2022) · cites this paper as [26]
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“In pancreatic beta cells, GLUT1, GLUT2 and GLUT3 are involved in glucose sensing and possess different affinities for extracellular glucose compared to those in fat and muscle cells (26, 28).”
From The progression of secondary diabetes: A review of modeling studies (2022) · cites this paper as [26]
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“GLUTs are also involved in glucose sensing in pancreatic beta cells, with the caveat that the GLUT isoforms present in these insulin-secreting cells possess a different glucose sensitivity threshold than those in fat and muscle cells ( 28-31 ).”
From Dynamic modulation of glucose utilisation by glucocorticoid rhythms in health and disease (2020) · cites this paper as [28]
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Metadata
- Authors
- Thorens, B., & Mueckler, M.
- Affiliations
- University of Lausanne (CH)
- Washington University in St. Louis (US)
- Corresponding author
- Mueckler, Mike
- ORCID
- Thorens, Bernard
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2010-02
- Volume
- 298
- Issue
- 2
- Pages
- E141-E145
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- PMC
- PMC2822486
- OpenAlex
- W2112331117
- Cited by
- 1,013
- References
- 51
- Citations by year
- 2026: 36 · 2025: 57 · 2024: 87 · 2023: 74 · 2022: 70 · 2021: 76 · 2020: 80 · 2019: 62 · 2018: 94 · 2017: 59 · 2016: 58 · 2015: 63 · 2014: 63 · 2013: 43 · 2012: 61
- FWCI
- 2.22
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Funders
- U.S. Public Health Service (R0143695)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Keywords
- glucose transporters, GLUT family, glucose homeostasis, fructose transport, urate transport, membrane transporters
- MeSH terms
- Glucose, Humans, Membrane Transport Proteins, Glucose Transport Proteins, Facilitative
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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