A connexin-32 mutation associated with Charcot-Marie-Tooth disease does not affect channel formation in oocytes

Cristina Rabadan-Diehl, Gerhard Dahl, Rudolf Werner

Research output: Contribution to journalArticle

64 Scopus citations

Abstract

Members of the connexin family differ most in their carboxy-termini, both with respect to sequence and length. In order to assess the contribution of this region to channel function, a series of carboxy-terminal deletion mutants were tested in the paired-oocyte expression system. Connexin-32 can be truncated by 64 amino acids without detectable loss of its known channel properties. Removal of additional amino acids results in a progressive loss of function over a stretch of 4 amino acids. In addition to this effect of length the charge of the carboxy-terminus appears to be another determinant of channel function. One of the fully functional deletion mutants, carrying a stop codon after amino acid-219, had been reported to be associated with Charcot-Marie-Tooth disease. The implications of this finding are discussed.

Original languageEnglish (US)
Pages (from-to)90-94
Number of pages5
JournalFEBS letters
Volume351
Issue number1
DOIs
StatePublished - Aug 29 1994

Keywords

  • Channel formation
  • Charcot-Marie-Tooth disease
  • Connexin-32
  • Deletion mutants
  • Gap junction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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