Structural Insights into the CFTR-NHERF Interaction

Structural Insights into the CFTR-NHERF Interaction J. Membrane Biol. 192, 79–88 (2003) DOI: 10.1007/s00232-002-1065-x Topical Review J.A.A. Ladias Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Division of Experimental Medicine, Harvard Institutes of Medicine, Harvard, Medical School, 4Blackfan Circle, Boston Massachusetts 02115, USA Received: 26 July 2002/Revised: 28 October 2002 Introduction mains may be expressed as separate polypeptides or half-transporters, such as the putative lipid A trans- The cystic fibrosis transmembrane conductance reg- porter MsbA from Escherichia coli [8], or fused to- ulator (CFTR) is a low-conductance chloride channel gether in a single polypeptide, as in the CFTR protein. located at the apical membrane of epithelial cells The energy of ATP binding and hydrolysis is used to where it mediates cAMP-dependent chloride secre- select and transport the substrates through the lipid tion (reviewed in [2, 23, 71]). Abnormal CFTR bilayer by unknown mechanisms. The current draft of function is associated with the pathogenesis of human the human genome sequence contains 48 ABC genes, diseases, including cystic fibrosis, secretory diarrhea, 16 of which encode transporters with known function, and pancreatitis [2, 20]. Cystic fibrosis is caused by including the multidrug resistance protein, the trans- mutations in the CFTR gene that decrease the cell porter for antigen presentation, http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Structural Insights into the CFTR-NHERF Interaction

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Publisher
Springer-Verlag
Copyright
Copyright © 2003 by Springer-Verlag New York Inc.
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-002-1065-x
Publisher site
See Article on Publisher Site

Abstract

J. Membrane Biol. 192, 79–88 (2003) DOI: 10.1007/s00232-002-1065-x Topical Review J.A.A. Ladias Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Division of Experimental Medicine, Harvard Institutes of Medicine, Harvard, Medical School, 4Blackfan Circle, Boston Massachusetts 02115, USA Received: 26 July 2002/Revised: 28 October 2002 Introduction mains may be expressed as separate polypeptides or half-transporters, such as the putative lipid A trans- The cystic fibrosis transmembrane conductance reg- porter MsbA from Escherichia coli [8], or fused to- ulator (CFTR) is a low-conductance chloride channel gether in a single polypeptide, as in the CFTR protein. located at the apical membrane of epithelial cells The energy of ATP binding and hydrolysis is used to where it mediates cAMP-dependent chloride secre- select and transport the substrates through the lipid tion (reviewed in [2, 23, 71]). Abnormal CFTR bilayer by unknown mechanisms. The current draft of function is associated with the pathogenesis of human the human genome sequence contains 48 ABC genes, diseases, including cystic fibrosis, secretory diarrhea, 16 of which encode transporters with known function, and pancreatitis [2, 20]. Cystic fibrosis is caused by including the multidrug resistance protein, the trans- mutations in the CFTR gene that decrease the cell porter for antigen presentation,

Journal

The Journal of Membrane BiologySpringer Journals

Published: Apr 1, 2003

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