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• W2092471036 abstract "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." @default.
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• W2092471036 date "2009-05-04" @default.
• W2092471036 modified "2023-10-15" @default.
• W2092471036 title "The role of<i>N</i>-glycosylation in transport function and surface targeting of the human solute carrier PAT1" @default.
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• W2092471036 doi "https://doi.org/10.1016/j.febslet.2009.04.037" @default.
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