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Effects of substitution of putative transmembrane segments on nicotinic acetylcholine receptor function
Author(s) -
Tobimatsu Takamasa,
Fujita Yoshihiko,
Fukuda Kazuhiko,
Tanaka Ken-ichi,
Mori Yasuo,
Konno Takashi,
Mishina Masayoshi,
Numa Shosaku
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80191-6
Subject(s) - transmembrane protein , transmembrane domain , nicotinic acetylcholine receptor , acetylcholine receptor , biology , muscarinic acetylcholine receptor m5 , biochemistry , torpedo , acetylcholine , microbiology and biotechnology , ganglion type nicotinic receptor , receptor , chemistry , muscarinic acetylcholine receptor m3 , pharmacology
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.