Handbook of Glycosyltransferases and Related Genes pp 1413-1421 | Cite as
UDP-N-Acetylglucosamine/UDP-Glucose/GDP-Mannose Transporter (HFRC1) (SLC35D2)
Glycosylation is carried out in the lumen of the endoplasmic reticulum (ER) or in the lumen of the Golgi apparatus by a range of glycosyltransferases. An activated form of sugar, termed a nucleotide sugar, commonly acts as the sugar donor. In higher organisms, nucleotide sugars are synthesized in the cytosol. Nucleotide sugar transporters, which are localized in the ER membrane or the Golgi membrane, transport nucleotide sugars from the cytosol into the lumen of the ER or the Golgi apparatus. Therefore, expression of nucleotide sugar transporters determines the glycosylation status of molecules on the cell surface and of secreted molecules.
UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter (UDP-GlcNAc/UDP-Glc/GDP-Man transporter), which is also known as human fringe connection 1 (HFRC1), has been cloned and its multi-substrate specific nucleotide sugar transport activity has been identified. HFRC1 is categorized as the second member of subgroup D of Solute carrier family 35 (SLC35D2). The hfrc1/SLC35D2 and SLC35D1 genes are orthologous to Drosophila frc and Caenorhabditis elegans sqv-7, suggesting that hfrc1/SLC35D2 and SLC35D1 share a common ancestral origin. Functional analyses of Drosophila Frc in vivo and of HFRC1/SLC35D2 in mammalian cell lines have shown that they have heparan sulfate-related activities. However, direct evidence linking defects in the activity of HFRC1 to human disease has not been obtained to date.
KeywordsGolgi Apparatus P2Y14 Receptor Nucleotide Sugar Solute Carrier Family Golgi Membrane
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