Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences.
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.
Napp
Joanna
J
Max Planck Institute for Experimental Medicine, Göttingen, Germany.
Monje
Francisco
F
Stühmer
Walter
W
Pardo
Luis A
LA
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
D051638:Ether-A-Go-Go Potassium Channels; D015221:Potassium Channels