Physiol Rev Ad Instruments
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Physiol. Rev. 79: 23-45, 1999;
0031-9333/99 $15.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by SHEPPARD, D. N.
Right arrow Articles by WELSH, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by SHEPPARD, D. N.
Right arrow Articles by WELSH, M. J.

PHYSIOLOGICAL REVIEWS   Vol. 79 No. 1 January 1999, pp. S23-S45
Copyright ©1999 The American Physiological Society

Structure and Function of the CFTR Chloride Channel

DAVID N. SHEPPARD AND MICHAEL J. WELSH

Human Genetics Unit, Department of Medicine, University of Edinburgh, Molecular Medicine Centre, Western General Hospital, Edinburgh, United Kingdom; and Howard Hughes Medical Institute, Departments of Internal Medicine and of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa

Sheppard, David N., and Michael J. Welsh. Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79, Suppl.: S23-S45, 1999. --- The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl- channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.




This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
G. Lamprecht and U. Seidler
The emerging role of PDZ adapter proteins for regulation of intestinal ion transport
Am J Physiol Gastrointest Liver Physiol, November 1, 2006; 291(5): G766 - G777.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. L. Berger, C. O. Randak, L. S. Ostedgaard, P. H. Karp, D. W. Vermeer, and M. J. Welsh
Curcumin Stimulates Cystic Fibrosis Transmembrane Conductance Regulator Cl- Channel Activity
J. Biol. Chem., February 18, 2005; 280(7): 5221 - 5226.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. G. Therien and C. M. Deber
Interhelical Packing in Detergent Micelles. FOLDING OF A CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR CONSTRUCT
J. Biol. Chem., February 15, 2002; 277(8): 6067 - 6072.
[Abstract] [Full Text] [PDF]

Home page
 J. Exp. Biol.Home page
K. O'Connor and K. Beyenbach
Chloride channels in apical membrane patches of stellate cells of Malpighian tubules of Aedes aegypti
J. Exp. Biol., January 1, 2001; 204(2): 367 - 378.
[Abstract] [PDF]

Home page
 J. Exp. Biol.Home page
N. McCarty
Permeation through the CFTR chloride channel
J. Exp. Biol., January 7, 2000; 203(13): 1947 - 1962.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Li, L. Salter-Cid, A. Vitiello, T. Preckel, J.-D. Lee, A. Angulo, Z. Cai, P. A. Peterson, and Y. Yang
Regulation of Transporter Associated with Antigen Processing by Phosphorylation
J. Biol. Chem., July 28, 2000; 275(31): 24130 - 24135.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. L. Berger and M. J. Welsh
Differences between Cystic Fibrosis Transmembrane Conductance Regulator and HisP in the Interaction with the Adenine Ring of ATP
J. Biol. Chem., September 15, 2000; 275(38): 29407 - 29412.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
O. Baldursson, L. S. Ostedgaard, T. Rokhlina, J. F. Cotten, and M. J. Welsh
Cystic Fibrosis Transmembrane Conductance Regulator Cl- Channels with R Domain Deletions and Translocations Show Phosphorylation-dependent and -independent Activity
J. Biol. Chem., January 12, 2001; 276(3): 1904 - 1910.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Cahill, M. W. Nason Jr., C. Ambrose, T.-Y. Yao, P. Thomas, and M. E. Egan
Identification of the Cystic Fibrosis Transmembrane Conductance Regulator Domains That Are Important for Interactions with ROMK2
J. Biol. Chem., May 26, 2000; 275(22): 16697 - 16701.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
X. C. Sun and J. A. Bonanno
Expression, localization, and functional evaluation of CFTR in bovine corneal endothelial cells
Am J Physiol Cell Physiol, April 1, 2002; 282(4): C673 - C683.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online