Effects of substitution of putative transmembrane segments on nicotinic acetylcholine receptor function

FEBS Letters

Fujita, Yoshihiko¹  Tobimatsu, Takamasa¹  Mishina, Masayoshi¹  Konno, Takashi¹  Numa, Shosaku¹  Tanaka, Ken-ichi¹  Fukuda, Kazuhiko¹  Mori, Yasuo¹ 

[1] Departments of Medical Chemistry and Molecular Genetics, Kyoto University Faculty of Medicine, Kyoto 606, Japan

关键词: Nicotinic acetylcholine receptor;    Transmembrane segment;    Site-directed mutagenesis;    cDNA expression;    Channel activity;    α-Bungarotoxin binding;    ACh;    acetylcholine;    AChR;    acetylcholine receptor;    α-BTX;    α-bungarotoxin;    VSV;    vesicular stomatitis virus;   

DOI  :  10.1016/0014-5793(87)80191-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mutants of the Torpedo nicotinic acetylcholine receptor in which each of the putative transmembrane segments of the α-subunit is replaced by the hydrophobic transmembrane segment of the vesicular stomatitis virus glycoprotein or of the human interleukin-2 receptor have been produced in Xenopus oocytes by cDNA manipulations. Functional analysis of these mutants shows that the hydrophobic segment M4 can be replaced by foreign transmembrane sequences without loss of channel activity. It is also suggested that the hydrophobic segments M1, M2 and M3 and the amphipathic segment MA are important for efficient expression of the acetylcholine receptor on the cell surface and that the specific amino acid sequence of segment M2 may be involved in channel activity.

【 授权许可】

Unknown