| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2048637 | FEBS Letters | 2011 | 5 Pages |
Nucleotide sugar transporters deliver substrates for glycosyltransferases into the endoplasmic reticulum and the Golgi apparatus. We demonstrated that overexpression of UDP-GlcNAc transporter (NGT) in MDCK-RCAr and CHO-Lec8 mutant cells defective in UDP-Gal transporter (UGT) restored galactosylation of N-glycans. NGT overexpression resulted in decreased transport of UDP-GlcNAc into the Golgi vesicles. This effect resembled the phenotype of mutant cells corrected by UGT1 overexpression. The transport of UDP-Gal was not significantly changed. Our data suggest that the biological function of UGT and NGT in galactosylation of macromolecules may be coupled.
► UDP-GlcNAc transporter (NGT) expression analyzed in cells defective in UDP-Gal transporter (UGT). ► Surprisingly overexpression of NGT partially restores galactosylation in UGT mutant cells. ► Biological function of UGT and NGT in galactosylation may be coupled.
