4.6 Article

N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK

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ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.12.056

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N-glycosylation; K2P channel; Potassium channel; Membrane targeting; Background potassium currents

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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. (C) 2009 Elsevier Inc. All rights reserved.

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