کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1932458 | 1050582 | 2010 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK](/preview/png/1932458.png)
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.
Journal: Biochemical and Biophysical Research Communications - Volume 391, Issue 2, 8 January 2010, Pages 1262–1267