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J Biol Chem, Vol. 274, Issue 6, 3602-3609, February 5, 1999
From the Department of Cell Biology, We previously demonstrated that the cystic
fibrosis transmembrane conductance regulator (CFTR) is rapidly
endocytosed in epithelial cells (Prince, L. S., Workman, R. B., Jr., and Marchase, R. B. (1994) Proc. Natl. Acad. Sci.
U. S. A. 91, 5192-5196). To determine the structural features
of CFTR required for endocytosis, we prepared chimeric molecules
consisting of the amino-terminal (residues 2-78) and carboxyl-terminal
tail regions (residues 1391-1476) of CFTR, each fused to the
transmembrane and extracellular domains of the transferrin receptor.
Functional analysis of the CFTR-(2-78) and CFTR-(1391-1476) indicated
that both chimeras were rapidly internalized. Deletion of residues
1440-1476 had no effect on chimera internalization. Mutations of
potential internalization signals in both cytoplasmic domains reveal
that only one mutation inhibits internalization, Y1424A. Using a
surface biotinylation reaction, we also examined internalization rates
of wild type and mutant CFTRs expressed in COS-7 cells. We found that
both wild type and A1440X CFTR were rapidly internalized,
whereas the Y1424A CFTR mutant, like the chimeric protein, had ~40%
reduced internalization activity. Deletions in the amino-terminal tail region of CFTR resulted in defective trafficking of CFTR out of the
endoplasmic reticulum to the cell surface, suggesting that an intact
amino terminus is critical for biosynthesis. In summary, our results
suggest that both tail regions of CFTR are sufficient to promote rapid
internalization of a reporter molecule and that tyrosine 1424 is
required for efficient CFTR endocytosis.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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