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

Takamasa Tobimatsu, Yoshihiko Fujita, Kazuhiko Fukuda, Ken ichi Tanaka, Yasuo Mori, Takashi Konno, Masayoshi Mishina, Shosaku Numa

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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.

Original languageEnglish
Pages (from-to)56-62
Number of pages7
JournalFEBS Letters
Issue number1
Publication statusPublished - Sep 28 1987



  • Channel activity
  • Nicotinic acetylcholine receptor
  • Site-directed mutagenesis
  • Transmembrane segment
  • cDNA expression
  • α-Bungarotoxin binding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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