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• W2040821685 abstract "Within the first external loop of mouse and human TRESK subunits one or two N-glycosylation consensus sites were identified, respectively. Using site directed mutagenesis and Western immunoblotting a single residue of both orthologues was found to be glycosylated upon heterologous expression. Two-electrode voltage-clamp recordings from Xenopus oocytes revealed that current amplitudes of N-glycosylation mutants were reduced by 80% as compared to wildtype TRESK. To investigate membrane targeting, GFP-tagged TRESK subunits were expressed in Xenopus oocytes and fluorescence intensity at the cell surface was measured by confocal microscopy. Signals of the N-glycosylation mutants were reduced by >50%, indicating that their lower current amplitudes substantially result from inadequate surface expression of the channel." @default.
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• W2040821685 date "2010-01-01" @default.
• W2040821685 modified "2023-09-23" @default.
• W2040821685 title "N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK" @default.
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• W2040821685 doi "https://doi.org/10.1016/j.bbrc.2009.12.056" @default.
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