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  • Title: N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK.
    Author: Egenberger B, Polleichtner G, Wischmeyer E, Döring F.
    Journal: Biochem Biophys Res Commun; 2010 Jan 08; 391(2):1262-7. PubMed ID: 20006580.
    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.
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