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Solute carrier family 2 (facilitated glucose transporter), member 1
Identifiers
Symbols SLC2A1; GLUT; GLUT1; MGC141895; MGC141896
External IDs OMIM138140 MGI95755 HomoloGene68520 GeneCards: SLC2A1 Gene
RNA expression pattern
PBB GE SLC2A1 201250 s at tn.png
PBB GE SLC2A1 201249 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6513 20525
Ensembl ENSG00000117394 ENSMUSG00000028645
UniProt P11166 Q3TD17
RefSeq (mRNA) NM_006516 NM_011400
RefSeq (protein) NP_006507 NP_035530
Location (UCSC) Chr 1:
43.16 - 43.2 Mb
Chr 4:
118.61 - 118.64 Mb
PubMed search [1] [2]

Glucose transporter 1, also known as GLUT1 or SLC2A1 is a protein which in humans is encoded by the SLC2A1 gene.[1] GLUT1 facilitates the transport of glucose across the plasma membranes of mammalian cells.[2]

Contents

Discovery

GLUT1 was the first glucose transporter to be characterized.[1]

Function

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 take-up 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.[3]

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.

Structure

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 signficance

Mutations in the GLUT1 gene are responsible for GLUT1 deficiency or De Vivo disease, which is a rare autosomal dominant disorder.[4] 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.[5]

Interactions

GLUT1 has been shown to interact with GIPC1.[6]

References

  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. doi:10.1126/science.3839598. PMID 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. doi:10.1146/annurev.nu.16.070196.001315. PMID 8839927. 
  3. ^ 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. doi:10.1016/j.cell.2008.01.042. Lay summary – ScienceDaily (2008-03-21). 
  4. ^ 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. doi:10.1038/ng0298-188. PMID 9462754. 
  5. ^ 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. doi:10.1016/S0092-8674(03)00881-X. PMID 14622599. http://linkinghub.elsevier.com/retrieve/pii/S009286740300881X. 
  6. ^ Bunn, R C; Jensen M A, Reed B C (Apr. 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell (UNITED STATES) 10 (4): 819–32. ISSN 1059-1524. PMID 10198040. 

Further reading

  • Hruz PW, Mueckler MM (2002). "Structural analysis of the GLUT1 facilitative glucose transporter (review).". Mol. Membr. Biol. 18 (3): 183–93. doi:10.1080/09687680110072140. PMID 11681785. 
  • Baumann MU, Deborde S, Illsley NP (2003). "Placental glucose transfer and fetal growth.". Endocrine 19 (1): 13–22. doi:10.1385/ENDO:19:1:13. PMID 12583599. 
  • 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

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