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J. Biol. Chem., Vol. 277, Issue 42, 40099-40105, October 18, 2002
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From the The C terminus of CFTR contains a PDZ interacting
domain that is required for the polarized expression of cystic fibrosis transmembrane conductance regulator (CFTR) in the apical plasma membrane of polarized epithelial cells. To elucidate the mechanism whereby the PDZ interacting domain mediates the polarized expression of
CFTR, Madin-Darby canine kidney cells were stably transfected with wild type (wt-CFTR) or C-terminally truncated human CFTR (CFTR- Dartmouth Medical School, Department of
Physiology, Hanover, New Hampshire 03755, the
§ Department of Cell Biology, University of Alabama,
Birmingham, Alabama 35294, the ¶ Johns Hopkins
University, Center for Medical Genetics, Johns Hopkins Hospital,
Baltimore, Maryland 21287, the Johns Hopkins University,
School of Medicine, Department of Physiology, Baltimore, Maryland
21205, and the ** Department of Biological Sciences,
Dartmouth College, Hanover, New Hampshire 03755
TRL). We tested the hypothesis that the PDZ interacting domain
regulates sorting of CFTR from the Golgi to the apical plasma membrane.
Pulse-chase studies in combination with domain-selective cell surface
biotinylation revealed that newly synthesized wt-CFTR and CFTR-TRL
were targeted equally to the apical and basolateral membranes in a
nonpolarized fashion. Thus, the PDZ interacting domain is not an apical
sorting motif. Deletion of the PDZ interacting domain reduced the
half-life of CFTR in the apical membrane from ~24 to ~13 h but had
no effect on the half-life of CFTR in the basolateral membrane. Thus,
the PDZ interacting domain is an apical membrane retention motif. Next,
we examined the hypothesis that the PDZ interacting domain affects the
apical membrane half-life of CFTR by altering its endocytosis and/or
endocytic recycling. Endocytosis of wt-CFTR and CFTR-TRL did not
differ. However, endocytic recycling of CFTR-TRL was decreased when
compared with wt-CFTR. Thus, deletion of the PDZ interacting domain
reduced the half-life of CFTR in the apical membrane by decreasing CFTR endocytic recycling. Our results identify a new role for PDZ proteins in regulating the endocytic recycling of CFTR in polarized epithelial cells.
To whom correspondence should be addressed: Dept. of
Physiology, Dartmouth Medical School, Hanover, NH 03755. E-mail:
Bruce. A.Stanton{at}Dartmouth.edu.
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