Effects of mutation at a conserved N‐glycosylation site in the bovine retinal cyclic nucleotide‐gated ion channel

FEBS Letters

Lee, Kyunglim²  Park, Chul-Seung¹  Lee, Han Mi¹  Rho, Seong-hwan¹ 

[1] Department of Life Science, Kwangju Institute of Science and Technology (K-JIST), Kwangju 500-712, South Korea;College of Pharmacy, Ewha Womans University, Seoul 120-750, South Korea

关键词: N-glycosylation;    Cyclic nucleotide-gated ion channel;    Guanosine 3′;    5′-cyclic mononucleotide;    Divalent cation blockade;    Xenopus oocyte;    CNG;    cyclic nucleotide-gated;    CNGC;    cyclic nucleotide-gated ion channel;    cGMP;    guanosine 3′;    5′-cyclic mononucleotide;    P-region;    pore-forming region;    I–V;    current–voltage;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/S0014-5793(00)01863-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown