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

Napp, J.; Monje, F.; Stuhmer, W.; Pardo, L. A.

doi:M504228200 [pii]
10.1074/jbc.M504228200

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

MPS-Authors

Napp, J.
Max Planck Society;

Monje, F.
Max Planck Society;

Stuhmer, W.
Max Planck Society;

Pardo, L. A.
Max Planck Society;

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Citation

Napp, J., Monje, F., Stuhmer, W., & Pardo, L. A. (2005). Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences. J Biol Chem, 280(33), 29506-12. doi:M504228200 [pii] 10.1074/jbc.M504228200.

Cite as: https://hdl.handle.net/21.11116/0000-0009-F21F-4

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.