| First Author | Egenberger B | Year | 2010 |
| Journal | Biochem Biophys Res Commun | Volume | 391 |
| Issue | 2 | Pages | 1262-7 |
| PubMed ID | 20006580 | Mgi Jnum | J:166001 |
| Mgi Id | MGI:4839430 | Doi | 10.1016/j.bbrc.2009.12.056 |
| Citation | Egenberger B, et al. (2010) N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK. Biochem Biophys Res Commun 391(2):1262-7 |
| abstractText | 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. |
