| N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK. | |
| | |
MedLine Citation:
|
PMID: 20006580 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
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. |
| | |
Authors:
|
Brigitte Egenberger; Georg Polleichtner; Erhard Wischmeyer; Frank D?ring |
Publication Detail:
|
Type: Journal Article Date: 2009-12-16 |
Journal Detail:
|
Title: Biochemical and biophysical research communications Volume: 391 ISSN: 1090-2104 ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2010 Jan |
Date Detail:
|
Created Date: 2010-01-27 Completed Date: 2010-03-08 Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
|
Languages: eng Pagination: 1262-7 Citation Subset: IM |
Copyright Information:
|
Copyright 2009 Elsevier Inc. All rights reserved. |
Affiliation:
|
Institute of Physiology, Department of Neurophysiology, University of W?rzburg, 97070 W?rzburg, Germany. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Animals Cell Membrane / metabolism* Glycosylation Humans Mice Molecular Sequence Data Oocytes Patch-Clamp Techniques Potassium Channels / genetics, metabolism* Xenopus |
| Chemical | |
Reg. No./Substance:
|
0/KCNK18 protein, human; 0/Potassium Channels; 0/Trik protein, mouse |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Significance of HLA class I antibody-induced antioxidant gene expression for endothelial cell protec...
Next Document: Fatty acids of membrane phospholipids in Drosophila melanogaster lines showing rapid and slow recove...