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Cited by 719Metabolism, Diabetes, and CancerIon Transport and Channel RegulationDrug Transport and Resistance Mechanisms

The extended GLUT-family of sugar/polyol transport facilitators: nomenclature, sequence characteristics, and potential function of its novel members

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Joost, Hans-Georg, Thorens, Bernard·2001·Molecular Membrane Biology
DOI 10.1080/09687680110090456
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Abstract

During the last 2 years, several novel genes that encode glucose transporter-like proteins have been identified and characterized. Because of their sequence similarity with GLUT1, these genes appear to belong to the family of solute carriers 2A (SLC2A, protein symbol GLUT). Sequence comparisons of all 13 family members allow the definition of characteristic sugar/polyol transporter signatures: (1) the presence of 12 membrane-spanning helices, (2) seven conserved glycine residues in the helices, (3) several basic and acidic residues at the intracellular surface of the proteins, (4) two conserved tryptophan residues, and (5) two conserved tyrosine residues. On the basis of sequence similarities and characteristic elements, the extended GLUT family can be divided into three subfamilies, namely class I (the previously known glucose transporters GLUT1-4), class II (the previously known fructose transporter GLUT5, the GLUT7, GLUT9 and GLUT11), and class III (GLUT6, 8, 10, 12, and the myo-inositol transporter HMIT1). Functional characteristics have been reported for some of the novel GLUTs. Like GLUT1-4, they exhibit a tissue/cell-specific expression (GLUT6, leukocytes, brain; GLUT8, testis, blastocysts, brain, muscle, adipocytes; GLUT9, liver, kidney; GLUT10, liver, pancreas; GLUT11, heart, skeletal muscle). GLUT6 and GLUT8 appear to be regulated by sub-cellular redistribution, because they are targeted to intra-cellular compartments by dileucine motifs in a dynamin dependent manner. Sugar transport has been reported for GLUT6, 8, and 11; HMIT1 has been shown to be a H+/myo-inositol co-transporter. Thus, the members of the extended GLUT family exhibit a surprisingly diverse substrate specificity, and the definition of sequence elements determining this substrate specificity will require a full functional characterization of all members.

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Crossref · 10.1080/09687680110090456

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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 [30]

    The “Sub-classes of the extended GLUT family” section (page unavailable) places GLUT2 in pancreatic islets and GLUT4 in muscle and adipose tissue, and says these transporters differ in glucose affinity. It does not say that GLUTs perform glucose sensing in beta cells or specify a difference in glucose-sensitivity thresholds between those cells and fat or muscle cells. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • GLUT-1 is the main expressed GLUT in red blood cell membrane and is not insulin dependent.

    “It could be explained by the fact that GLUT-1 is the main expressed GLUT in red blood cell (RBC) membrane which is not insulin dependent [22,110]; thus, insulin resistance would not affect FDG uptake in RBCs.”

    From Effect of blood glucose level on standardized uptake value (SUV) in 18F-FDG PET-scan: a systematic review and meta-analysis of 20,807 individual SUV measurements (2019) · cites this paper as [110]

    The Introduction (page unavailable) says GLUT1 transports glucose into erythrocytes, and “Sub-classes of the extended GLUT family” lists erythrocytes among GLUT1’s characteristic tissues. The paper does not explicitly say GLUT1 is the main transporter in red blood cell membranes or that its activity there is insulin-independent; it discusses insulin-sensitive localization for GLUT4 instead. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

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Cites

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Research works printed but not linked: 11

  1. [2]2. Carayannopoulos, M. O., Chi, M. M. Y., Cui, Y., Pingsterhaus, J. M., McKnight, R. A., Mueckler, M., Devaskar, S. U. and Moley, K. H. 2000, GLUT8 is a glucose transporter responsible for insulin- stimulated glucose uptake in the blastocyst. Proceedings of the National Academy of Sciences (USA), 13, 7313 ± 7318.
  2. [4]4. Doege, H., Bocianski, A., Scheepers, A., Axer, H., Eckel, J., Joost, H. G. and SchuÈ rmann, A. 2001a, Characterization of the human glucose transporter GLUT11, a novel sugar transport facilitator specifically expressed in heart and skeletal muscle. Biochemical Journal, 359, 443 ± 449.
  3. [6]6. Doege, H., SchuÈ rmann, A., Bahrenberg, G., Brauers, A. and Joost, H. G. 2000b, Glucose transporter 8 (GLUT): a novel sugar transport facilitator with glucose transport activity. Journal of Biological Chemistry, 275, 16275 ± 16280.
  4. [9]9. Fukumoto, H., Seino, S., Imura, H., Seino, Y., Eddy, R. L., Fukushima, Y., Byers, M. G., Shows, T. B. and Bell, G. I. 1988, Sequence, tissue distribution, and chromosomal localization of mRNA encoding a human glucose transporter-like protein. Proceedings of the National Academy of Sciences (USA), 85, 5434± 5438.
  5. [11]11. Gould, G. W. and Holman, G. D. 1993, Facilitative glucose transporters: structure, function and tissue-specific expression. Biochemical Journal, 295, 329 ± 341.
  6. [15]15. Hresko, R., Kruse, M. and Mueckler, M. 1994, Topology of the GLUT1 glucose transporter deduced from glykosylation-scanning mutagenesis. Journal of Biological Chemistry, 269, 20482 ± 20488.
  7. [18]18. Joost, H. G., Bell, G. I., Best, J. D., Birnbaum, M. J., Charron, M. J., Chen, Y. T., Doege, H., James, D. E., Lodish, H., Moley, K. H., Moley, J. F., Mueckler, M., Rogers, S., Schu È rmann, A., Seino, S. and Thorens, B. 2001a, Nomenslature of the GLUT/SLC2A Family of Sugar/Polyol Transport Facilitators . American Journal of Physiology, in press.
  8. [19]19. Joost, H. G., Doege, H., Bocianski, A. and SchuÈ rmann, A. 2001b, Letter: Nomenclature of the GLUT family of sugar transport facilitators . GLUT6, GLUT9, GLUT10, and GLUT11. Biochemical Journal, 358, 791 ± 792.
  9. [21]21. Kayano T., Fukumoto, H., Eddy, R. L., Fan, Y. S., Byers, M. G., Shows, T. B. and Bell, G. I. 1988, Evidence for a family of human glucose transporter-lik e proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues. Journal of Biological Chemistry, 263, 15245 ± 15248.
  10. [25]25. Mori, H., Hashiramoto, M., Clark, A. E., Yang, J., Muraoka, A., Tamori, Y., Kasuga, M. and Holman, G. D. 1994, Substitution of tyrosine 293 of GLUT1 locks the transporter in an outward facing conformation. Journal of Biological Chemistry, 269, 11578 ± 11583.
  11. [31]31. Saier, M. H., Beatty, J. T., Goffeau, A., Harley, K. T., Heijne, W. H., Huang, S. C., Jack, D. L., Jahn, P. S., Lew, K., Liu, J., Pao, S. S., Paulsen, I. T., Tseng, T. T. and Virk, P. S. 1999, The major transporter facilitator superfamily. Journal of Molecular Microbiol- ogy and Biotechnology, 1, 257 ± 279.

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Authors
Joost, H.-G., & Thorens, B.
Affiliations
  • RWTH Aachen University (DE)
  • University of Lausanne (CH)
ORCID
Venue
Molecular Membrane Biology
Publisher
Informa UK Limited
Published
2001-01
Volume
18
Issue
4
Pages
247-256
ISSN
  • 0968-7688 (ISSN-L)
  • 1464-5203
DOI
10.1080/09687680110090456
OpenAlex
W2111158723
Cited by
719
References
28
Citations by year
2026: 7 · 2025: 19 · 2024: 14 · 2023: 20 · 2022: 28 · 2021: 27 · 2020: 23 · 2019: 21 · 2018: 17 · 2017: 20 · 2016: 28 · 2015: 32 · 2014: 21 · 2013: 40 · 2012: 29
FWCI
11.87
Type
journal article
Language
en
Open access
Locations
  • Molecular Membrane Biology (publishedVersion)
  • PubMed (publishedVersion)
  • IRIS (submittedVersion)
  • RWTH Publications (RWTH Aachen) (submittedVersion)
  • SERVAL (Université de Lausanne) (submittedVersion)
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
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords
GLUT family, sugar transporters, GLUT8, GLUT9, GLUT10, GLUT5, GLUT1, GLUT4, myo-inositol transporter, subcellular targeting, dileucine motif, dynamin, substrate specificity, tissue-specific gene expression, protein nomenclature, sequence motifs
MeSH terms
Amino Acid Sequence, Animals, Cloning, Molecular, Humans, Molecular Sequence Data, Monosaccharide Transport Proteins, Terminology as Topic, Tissue Distribution, Consensus Sequence, Sequence Alignment, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Isoforms, Amino Acid Motifs

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