Journal article

Conserved Glu-47 and Lys-50 residues are critical for UDP-N-acetylglucosamine/UMP antiport activity of the mouse Golgi-associated transporter Slc35a3

M Agustina Toscanini, M Belen Favarolo, F Luis Gonzalez Flecha, Berit Ebert, Carsten Rautengarten, Luis M Bredeston

JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2019

Abstract

Nucleotide sugar transporters (NSTs) regulate the flux of activated sugars from the cytosol into the lumen of the Golgi apparatus where glycosyltransferases use them for the modification of proteins, lipids, and proteoglycans. It has been well-established that NSTs are antiporters that exchange nucleotide sugars with the respective nucleoside monophosphate. Nevertheless, information about the molecular basis of ligand recognition and transport is scarce. Here, using topology predictors, cysteine-scanning mutagenesis, expression of GFP-tagged protein variants, and phenotypic complementation of the yeast strain Kl3, we identified residues involved in the activity of a mouse UDP-GlcNAc transpor..

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Grants

Awarded by National Research Council (CONICET, Argentina)


Awarded by Australian Research Council


Awarded by Mizutani Foundation for Glycoscience


Funding Acknowledgements

This work was supported by the National Research Council (CONICET, Argentina) Grant PIP-11220090100811, and University of Buenos Aires Travel Award (to L. M. B.). The authors declare that they have no conflicts of interest with the contents of this article.Supported by Australian Research Council Future Fellowship FT160100276, Discovery Grant DP180102630 and Mizutani Foundation for Glycoscience Grant 18-0237.