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

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.

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 Creators:
Napp, J.1, Author
Monje, F.1, Author
Stuhmer, W.1, Author
Pardo, L. A.1, Author
Affiliations:
1Max Planck Society, ou_persistent13              

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Free keywords: Animals CHO Cells Cricetinae Ether-A-Go-Go Potassium Channels Glycosylation Potassium Channels/chemistry/*physiology Protein Processing, Post-Translational Protein Transport Xenopus
 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.

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Language(s): eng - English
 Dates: 2005-08-192005-06-21
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: 15964838
DOI: M504228200 [pii] 10.1074/jbc.M504228200
ISSN: 0021-9258 (Print) 0021-9258 (Linking)
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Title: J Biol Chem
Source Genre: Journal
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Pages: - Volume / Issue: 280 (33) Sequence Number: - Start / End Page: 29506 - 12 Identifier: -