Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-1739
J Biol Chem 2005 Aug 19;28033:29506-12. doi: 10.1074/jbc.M504228200.
Show Gene links Show Anatomy links

Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences.

Napp J , Monje F , Stühmer W , Pardo LA .


???displayArticle.abstract???
N-Linked glycosylation is a common post-translational modification of membrane proteins. Here we report that mature Eag1 potassium channels carry sugar moieties linked to asparagines at positions 388 and 406. Asn-388 seems to undergo only core glycosylation, but complex sugars are bound to Asn-406. Correct complex glycosylation is required for proper trafficking of Eag1 to the plasma membrane but is also crucial for the correct function of channels already inserted in the membrane.

???displayArticle.pubmedLink??? 15964838
???displayArticle.link??? J Biol Chem


Species referenced: Xenopus
Genes referenced: kcnh1