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

FEBS Letters

Rabadan-Diehl, Cristina¹  Dahl, Gerhard¹  Werner, Rudolf¹ 

[1] Biochemistry and Molecular Biology and Departments of Physiology and Biophysics, University of Miami, School of Medicine, PO Box 016430, Miami, FL 33101, USA

关键词: Connexin-32;    Gap junction;    Deletion mutants;    Channel formation;    Charcot-Marie-Tooth disease;   

DOI  :  10.1016/0014-5793(94)00819-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown