The SLC2 (GLUT) family of membrane transporters
Open accessAbstract
GLUT proteins are encoded by the SLC2 genes and are members of the major facilitator superfamily of membrane transporters. Fourteen GLUT proteins are expressed in the human and they are categorized into three classes based on sequence similarity. All GLUTs appear to transport hexoses or polyols when expressed ectopically, but the primary physiological substrates for several of the GLUTs remain uncertain. GLUTs 1-5 are the most thoroughly studied and all have well established roles as glucose and/or fructose transporters in various tissues and cell types. The GLUT proteins are comprised of ∼500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 membrane-spanning domains. In this review we briefly describe the major characteristics of the 14 GLUT family members.
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GLUTs are involved in glucose sensing in pancreatic beta cells, and the GLUT isoforms in these insulin-secreting cells have a different glucose sensitivity threshold than those in fat and muscle cells.
“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 [29]
The GLUT2 section (page unavailable) identifies GLUT2 as the major transporter in rodent beta cells and says glucose uptake is the first step in glucose-stimulated insulin secretion. It also describes GLUT2’s unusually low glucose affinity, while the GLUT4 section identifies GLUT4 in fat and muscle. But the paper does not establish a different beta-cell glucose-sensing threshold caused by those isoforms: it says glucokinase, rather than glucose transport, is usually rate-limiting, and notes that human islets also express GLUT1 and GLUT3. (LLM, conf=0.85)
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Ugbode, C., Hu, Y., Whalley, B., Peers, C., Rattray, M., & Dallas, M. L. (2017) · Biochemical Journal · doi:10.1042/bcj20160505 · Cited by 25 · see citing works
Dynamic modulation of glucose utilisation by glucocorticoid rhythms in health and disease
Zavala, E., Gil-Gómez, C. A., Wedgwood, K. C. A., Burgess, R., Tsaneva-Atanasova, K., & Herrera-Valdez, M. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.27.968354 · Cited by 8 · see citing works
- Authors
- Mueckler, M., & Thorens, B.
- Affiliations
- Washington University in St. Louis (US)
- University of Lausanne (CH)
- Corresponding author
- Mueckler, Mike
- ORCID
- Thorens, Bernard
- Venue
- Molecular Aspects of Medicine
- Publisher
- Elsevier BV
- Published
- 2013-04
- Volume
- 34
- Issue
- 2-3
- Pages
- 121-138
- ISSN
- 0098-2997 (ISSN-L)
- PMC
- PMC4104978
- OpenAlex
- W2030324194
- Cited by
- 1,328
- References
- 178
- Citations by year
- 2026: 83 · 2025: 112 · 2024: 133 · 2023: 116 · 2022: 138 · 2021: 131 · 2020: 134 · 2019: 108 · 2018: 107 · 2017: 78 · 2016: 62 · 2015: 69 · 2014: 47 · 2013: 9
- FWCI
- 5.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Aspects of Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion, other-oa)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (113525, 31003A)
- National Institutes of Health
- U.S. Public Health Service (R0143695)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK085110, R01DK043695, P30DK020579)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Keywords
- major facilitator superfamily, membrane transporters, glucose transporters, fructose transporter, hexose transport, GLUT1, GLUT5, N-glycans, transporter structure
- MeSH terms
- Amino Acid Sequence, Biological Transport, Multigene Family, Hexoses, Humans, Models, Biological, Models, Molecular, Molecular Sequence Data, Polymers, Protein Conformation, Molecular Structure, Protein Structure, Tertiary, Glucose Transport Proteins, Facilitative
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