期刊
FEBS LETTERS
卷 583, 期 10, 页码 1631-1636出版社
WILEY
DOI: 10.1016/j.febslet.2009.04.037
关键词
hPAT1; Solute carrier; Glycosylation; Peptide: N-glycosidase F; Xenopus laevis oocyte
资金
- State Saxony-Anhalt Life Sciences Excellence Initiative [XB3599HP/0105T]
- Deutsche Forschungsgemeinschaft [BR 2430/4-3]
In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470. To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes. Single replacements of asparagine residues had no effect on transport activity. However, multiple substitutions resulted in a decreased transport rate, leaving K-t unchanged. Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants. This indicates that N-glycans are not required for transport function, but are important for membrane targeting. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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