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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Egenberger B,Polleichtner G,Wischmeyer E,Döring F

doi

10.1016/j.bbrc.2009.12.056

subject

Has Abstract

pub_date

2010-01-08 00:00:00

pages

1262-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)02429-2

journal_volume

391

pub_type

杂志文章

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