Journal of Bioenergetics and Biomembranes

, Volume 29, Issue 5, pp 443–451

CFTR: Domains, Structure, and Function

Authors

  • Sreenivas Devidas
    • Department of Physiology and PediatricsJohns Hopkins University School of Medicine
  • William B. Guggino
    • Department of Physiology and PediatricsJohns Hopkins University School of Medicine
Article

DOI: 10.1023/A:1022430906284

Cite this article as:
Devidas, S. & Guggino, W.B. J Bioenerg Biomembr (1997) 29: 443. doi:10.1023/A:1022430906284

Abstract

Mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR) cause cystic fibrosis (CF) (Collins, 1992). Over 500 naturally occurring mutations have been identified in CF gene which are located in all of the domains of the protein (Kerem et al., 1990; Mercier et al., 1993; Ghanem et al., 1994; Fanen et al., 1992; Ferec et al., 1992; Cutting et al., 1990). Early studies by several investigators characterized CFTR as a chloride channel (Anderson et al.; 1991b,c; Bear et al., 1991). The complex secondary structure of the protein suggested that CFTR might possess other functions in addition to being a chloride channel. Studies have established that the CFTR functions not only as a chloride channel but is indeed a regulator of sodium channels (Stutts et al., 1995), outwardly rectifying chloride channels (ORCC) (Gray et al., 1989; Garber et al., 1992; Egan et al., 1992; Hwang et al., 1989; Schwiebert et al., 1995) and also the transport of ATP (Schwiebert et al., 1995; Reisin et al., 1994). This mini-review deals with the studies which elucidate the functions of the various domains of CFTR, namely the transmembrane domains, TMD1 and TMD2, the two cytoplasmic nucleotide binding domains, NBD1 and NBD2, and the regulatory, R, domain.

Chloride channelsCFoutwardly rectifying chloride channelsCFTRreview

Copyright information

© Plenum Publishing Corporation 1997