| First Author | Wang S | Year | 2000 |
| Journal | Cell | Volume | 103 |
| Issue | 1 | Pages | 169-79 |
| PubMed ID | 11051556 | Mgi Jnum | J:230388 |
| Mgi Id | MGI:5758841 | Doi | 10.1016/s0092-8674(00)00096-9 |
| Citation | Wang S, et al. (2000) Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism to potentiate the chloride channel activity. Cell 103(1):169-79 |
| abstractText | The cystic fibrosis transmembrane conductance regulator (CFTR) gene encodes a chloride channel protein that belongs to the superfamily of ATP binding cassette (ABC) transporters. Phosphorylation by protein kinase A in the presence of ATP activates the CFTR-mediated chloride conductance of the apical membranes. We have identified a novel hydrophilic CFTR binding protein, CAP70, which is also concentrated on the apical surfaces. CAP70 consists of four PDZ domains, three of which are capable of binding to the CFTR C terminus. Linking at least two CFTR molecules via cytoplasmic C-terminal binding by either multivalent CAP70 or a bivalent monoclonal antibody potentiates the CFTR chloride channel activity. Thus, the CFTR channel can be switched to a more active conducting state via a modification of intermolecular CFTR-CFTR contact that is enhanced by an accessory protein. |
