title: Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences.
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.
authors.affiliation: Max Planck Institute for Experimental Medicine, Göttingen, Germany.
authors.forename: Joanna
authors.initials: J
authors.lastname: Napp
authors.forename: Francisco
authors.initials: F
authors.lastname: Monje
authors.forename: Walter
authors.initials: W
authors.lastname: Stühmer
authors.forename: Luis A
authors.initials: LA
authors.lastname: Pardo
mesh_terms: D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D051638:Ether-A-Go-Go Potassium Channels; D006031:Glycosylation; D015221:Potassium Channels / Q000737:chemistry / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D021381:Protein Transport; D014981:Xenopus
chemical_list: D051638:Ether-A-Go-Go Potassium Channels; D015221:Potassium Channels