TY - JOUR
T1 - CFTR
T2 - Domains, structure, and function
AU - Devidas, Sreenivas
AU - Guggino, William B.
N1 - Funding Information:
This work was supported by the Cystic Fibrosis Foundation Research Development Program and National Institutes of Health Grants Nos. HL 51811, HL 47122, and DK 48977 to WBG.
PY - 1997
Y1 - 1997
N2 - 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,; 1991 b,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, TMDI and TMD2, the two cytoplasmic nucleotide binding domains, NBDI and NBD2, and the regulatory, R, domain.
AB - 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,; 1991 b,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, TMDI and TMD2, the two cytoplasmic nucleotide binding domains, NBDI and NBD2, and the regulatory, R, domain.
KW - CF
KW - CFTR
KW - Chloride channels
KW - Outwardly rectifying chloride channels
KW - Review
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U2 - 10.1023/A:1022430906284
DO - 10.1023/A:1022430906284
M3 - Short survey
C2 - 9511929
AN - SCOPUS:0031425728
SN - 0145-479X
VL - 29
SP - 443
EP - 451
JO - Journal of Bioenergetics and Biomembranes
JF - Journal of Bioenergetics and Biomembranes
IS - 5
ER -