Open Access Articles- Top Results for GLUT1


External IDsOMIM138140 MGI95755 HomoloGene68520 IUPHAR: 875 ChEMBL: 2535 GeneCards: SLC2A1 Gene
RNA expression pattern
File:PBB GE SLC2A1 201250 s at tn.png
File:PBB GE SLC2A1 201249 at tn.png
More reference expression data
RefSeq (mRNA)NM_006516NM_011400
RefSeq (protein)NP_006507NP_035530
Location (UCSC)Chr 1:
43.39 – 43.42 Mb
Chr 4:
119.11 – 119.14 Mb
PubMed search[1][2]

Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is a uniporter protein that in humans is encoded by the SLC2A1 gene.[1] GLUT1 facilitates the transport of glucose across the plasma membranes of mammalian cells.[2]


GLUT1 was the first glucose transporter to be characterized. GLUT 1 is highly conserved.[1] GLUT 1 of humans and mouse has 98% homology. GLUT 1 has 40% homology with other GLUTs.


Energy-yielding metabolism in erythrocytes depends on a constant supply of glucose from the blood plasma, where the glucose concentration is maintained at about 5mM. Glucose enters the erythrocyte by facilitated diffusion via a specific glucose transporter, at a rate about 50,000 times greater than uncatalyzed transmembrane diffusion. The glucose transporter of erythrocytes (called GLUT1 to distinguish it from related glucose transporters in other tissues) is a type III integral protein with 12 hydrophobic segments, each of which is believed to form a membrane-spanning helix. The detailed structure of GLUT1 is not known yet, but one plausible model suggests that the side-by-side assembly of several helices produces a transmembrane channel lined with hydrophilic residues that can hydrogen-bond with glucose as it moves through the channel.[3]

GLUT1 is responsible for the low-level of basal glucose uptake required to sustain respiration in all cells. Expression levels of GLUT1 in cell membranes are increased by reduced glucose levels and decreased by increased glucose levels.

GLUT1 is also a major receptor for uptake of Vitamin C as well as glucose, especially in non vitamin C producing mammals as part of an adaptation to compensate by participating in a Vitamin C recycling process. In mammals that do produce Vitamin C, GLUT4 is often expressed instead of GLUT1.[4]

Tissue distribution

It is widely distributed in fetal tissues. In the adult it is expressed at highest levels in erythrocytes and also in the endothelial cells of barrier tissues such as the blood–brain barrier.


GLUT1 behaves as a Michaelis-Menten enzyme and contains 12 membrane-spanning alpha helices, each containing 20 amino acid residues. A helical wheel analysis shows that the membrane spanning alpha helices are amphipathic, with one side being polar and the other side hydrophobic. Six of these membrane spanning helices are believed to bind together in the membrane to create a polar channel in the center through which glucose can traverse, with the hydrophobic regions on the outside of the channel adjacent to the fatty acid tails of the membrane.

Clinical significance

Mutations in the GLUT1 gene are responsible for GLUT1 deficiency or De Vivo disease, which is a rare autosomal dominant disorder.[5] This disease is characterized by a low cerebrospinal fluid glucose concentration (hypoglycorrhachia), a type of neuroglycopenia, which results from impaired glucose transport across the blood–brain barrier.

GLUT1 is also a receptor used by the HTLV virus to gain entry into target cells.[6]

Glut1 has also been demonstrated as a powerful histochemical marker for haemangioma of infancy[7]


GLUT1 has been shown to interact with GIPC1.[8]

GLUT1 has two significant types in brain 45k and 55k. GLUT1 45k is present on astroglia of neurons and GLUT1 55k is present on capillaries in brain and is responsible for glucose transport across blood brain barrier and its deficiency causes low level of glucose in CSF(less than 60 mg/dl) which may manifest as convulsion in deficient individuals.

Recently it has been described a GLUT1 inhibitor, DERL3, that is often methylated in colorectal cancer. In this cancer, DERL3 methylations seems to mediate the Warburg Effect.[9]


Fasentin is a small molecule inhibitor of the intracellular domain of GLUT1 preventing glucose uptake.[10]

Interactive pathway map

Template:GlycolysisGluconeogenesis WP534


  1. ^ a b Mueckler M, Caruso C, Baldwin SA, Panico M, Blench I, Morris HR, Allard WJ, Lienhard GE, Lodish HF (September 1985). "Sequence and structure of a human glucose transporter". Science 229 (4717): 941–5. PMID 3839598. doi:10.1126/science.3839598. 
  2. ^ Olson AL, Pessin JE (1996). "Structure, function, and regulation of the mammalian facilitative glucose transporter gene family". Annu. Rev. Nutr. 16: 235–56. PMID 8839927. doi:10.1146/ 
  3. ^ Nelson DL, Cox MM (2008). Lehninger, Principles of Biochemistry. W. H. Freeman and Company. ISBN 978-0-7167-7108-1. 
  4. ^ Montel-hagen A, Kinet S, Manel N et al. (2008). "Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C". Cell 132 (6): 1039–1048. PMID 18358815. doi:10.1016/j.cell.2008.01.042. Lay summaryScienceDaily (2008-03-21). 
  5. ^ Seidner G, Alvarez MG, Yeh JI et al. (1998). "GLUT-1 deficiency syndrome caused by haploinsufficiency of the blood–brain barrier hexose carrier". Nat. Genet. 18 (2): 188–91. PMID 9462754. doi:10.1038/ng0298-188. 
  6. ^ Manel N, Kim FJ, Kinet S, Taylor N, Sitbon M, Battini JL (November 2003). "The ubiquitous glucose transporter GLUT-1 is a receptor for HTLV". Cell 115 (4): 449–59. PMID 14622599. doi:10.1016/S0092-8674(03)00881-X. 
  7. ^ North PE, Waner M, Mizeracki A, Mihm MC (January 2000). "GLUT1: a newly discovered immunohistochemical marker for juvenile hemangiomas". Hum. Pathol. 31 (1): 11–22. PMID 10665907. doi:10.1016/S0046-8177(00)80192-6. 
  8. ^ Bunn RC, Jensen MA, Reed BC (April 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell 10 (4): 819–32. PMC 25204. PMID 10198040. doi:10.1091/mbc.10.4.819. 
  9. ^ Lopez-Serra, P. et al. A DERL3-associated defect in the degradation of SLC2A1 mediates the Warburg effect. Nat. Commun. 5:3608 doi: 10.1038/ncomms4608 (2014).
  10. ^ Wood TE, Dalili S, Simpson CD, Hurren R, Mao X, Saiz FS et al. (2008). "A novel inhibitor of glucose uptake sensitizes cells to FAS-induced cell death". Mol. Cancer Ther. 7 (11): 3546–55. PMID 19001437. doi:10.1158/1535-7163.MCT-08-0569. Retrieved 2015-04-25. 

Further reading

  • North PE, Waner M, Mizeracki A, Mihm MC (January 2000). "GLUT1: a newly discovered immunohistochemical marker for juvenile hemangiomas". Hum. Pathol. 31 (1): 11–22. PMID 10665907. doi:10.1016/S0046-8177(00)80192-6. 
  • Hruz PW, Mueckler MM (2002). "Structural analysis of the GLUT1 facilitative glucose transporter (review).". Mol. Membr. Biol. 18 (3): 183–93. PMID 11681785. doi:10.1080/09687680110072140. 
  • Baumann MU, Deborde S, Illsley NP (2003). "Placental glucose transfer and fetal growth.". Endocrine 19 (1): 13–22. PMID 12583599. doi:10.1385/ENDO:19:1:13. 
  • Mobasheri A, Richardson S, Mobasheri R et al. (2006). "Hypoxia inducible factor-1 and facilitative glucose transporters GLUT1 and GLUT3: putative molecular components of the oxygen and glucose sensing apparatus in articular chondrocytes.". Histol. Histopathol. 20 (4): 1327–38. PMID 16136514. 

External links