| First Author | Ng BG | Year | 2023 |
| Journal | J Biol Chem | Volume | 299 |
| Issue | 1 | Pages | 102738 |
| PubMed ID | 36423686 | Mgi Jnum | J:354422 |
| Mgi Id | MGI:7734816 | Doi | 10.1016/j.jbc.2022.102738 |
| Citation | Ng BG, et al. (2023) GLUT1 is a highly efficient L-fucose transporter. J Biol Chem 299(1):102738 |
| abstractText | Understanding L-fucose metabolism is important because it is used as a therapy for several congenital disorders of glycosylation. Exogenous L-fucose can be activated and incorporated directly into multiple N- and O-glycans via the fucose salvage/recycling pathway. However, unlike for other monosaccharides, no mammalian L-fucose transporter has been identified. Here, we functionally screened nearly 140 annotated transporters and identified GLUT1 (SLC2A1) as an L-fucose transporter. We confirmed this assignment using multiple approaches to alter GLUT1 function, including chemical inhibition, siRNA knockdown, and gene KO. Collectively, all methods demonstrate that GLUT1 contributes significantly to L-fucose uptake and its utilization at low micromolar levels. Surprisingly, millimolar levels of D-glucose do not compete with L-fucose uptake. We also show macropinocytosis, but not other endocytic pathways, can contribute to L-fucose uptake and utilization. In conclusion, we determined that GLUT1 functions as the previously missing transporter component in mammalian L-fucose metabolism. |
