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A Pdz-Interacting Domain In Cftr Is An Apical Membrane Polarization Signal, Bryan D. Moyer, Jerod Denton, Katherine H. Karlson, Donna Reynolds, Shusheng Wang, John E. Mickle, Michael Milewski, Garry R. Cutting, William B. Guggino, Min Li, Bruce A. Stanton
A Pdz-Interacting Domain In Cftr Is An Apical Membrane Polarization Signal, Bryan D. Moyer, Jerod Denton, Katherine H. Karlson, Donna Reynolds, Shusheng Wang, John E. Mickle, Michael Milewski, Garry R. Cutting, William B. Guggino, Min Li, Bruce A. Stanton
Dartmouth Scholarship
Polarization of the cystic fibrosis transmembrane conductance regulator (CFTR), a cAMP-activated chloride channel, to the apical plasma membrane of epithelial cells is critical for vectorial transport of chloride in a variety of epithelia, including the airway, pancreas, intestine, and kidney. However, the motifs that localize CFTR to the apical membrane are unknown. We report that the last 3 amino acids in the COOH-terminus of CFTR (T-R-L) comprise a PDZ-interacting domain that is required for the polarization of CFTR to the apical plasma membrane in human airway and kidney epithelial cells. In addition, the CFTR mutant, S1455X, which lacks the 26 …