Abstract
Bovine retinal cyclic nucleotide-gated (CNG) ion channel contains an evolutionary conserved N-glycosylation site in the external loop between the fifth transmembrane segment and the pore-forming region. The effect of tunicamycin treatment and the site-specific mutation suggested that the channel is glycosylated when expressed in Xenopus oocytes. To test the role of glycosylation in this channel, N-glycosylation was abolished by mutation, and the detailed permeation and the gating characteristics of the mutant channel were investigated. The charge contribution turned out to be detectable, although the mutation of the N-glycosylation site did not affect expression and functionality of the CNG channel in oocytes. (C) 2000 Federation of European Biochemical Societies.
| Original language | English |
|---|---|
| Pages (from-to) | 246-252 |
| Number of pages | 7 |
| Journal | FEBS Letters |
| Volume | 478 |
| Issue number | 3 |
| DOIs | |
| State | Published - 4 Aug 2000 |
Bibliographical note
Funding Information:The authors wish to thank members of Neuro-biochemistry Laboratory at K-JIST for their timely helps throughout the work. This research was supported by the Grants from the Korea Research Foundation (F00040) and the Ministry of Education (BK21), Korea, to C.-S.P.
Keywords
- Cyclic nucleotide-gated ion channel
- Divalent cation blockade
- Guanosine 3',5'- cyclic mononucleotide
- N-glycosylation
- Xenopus oocyte