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J. Biol. Chem., Vol. 277, Issue 13, 11401-11409, March 29, 2002
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From the Departments of Cell and Molecular Biology, The Scripps
Research Institute, La Jolla, California 92037, the
§ Institute for Childhood and Neglected Diseases, and
The mechanism(s) of cystic fibrosis transmembrane
conductance regulator (CFTR) trafficking from the endoplasmic reticulum (ER) through the Golgi apparatus, the step impaired in individuals afflicted with the prevalent CFTR-
Non-conventional Trafficking of the Cystic Fibrosis
Transmembrane Conductance Regulator through the Early Secretory
Pathway*
, and Mayo Foundation and S. C. Johnson Medical Research
Center, Mayo Clinic, Scottsdale, Arizona 85259
F508 mutation leading to cystic fibrosis, is largely unknown. Recent morphological observations suggested that CFTR is largely absent from the Golgi in
situ (Bannykh, S. I., Bannykh, G. I., Fish, K. N.,
Moyer, B. D., Riordan, J. R., and Balch, W. E. (2000)
Traffic 1, 852-870), raising the possibility of a novel
trafficking pathway through the early secretory pathway. We now report
that export of CFTR from the ER is regulated by the conventional coat
protein complex II (COPII) in all cell types tested. Remarkably, in a
cell type-specific manner, processing of CFTR from the
core-glycosylated (band B) ER form to the complex-glycosylated (band C)
isoform followed a non-conventional pathway that was insensitive to
dominant negative Arf1, Rab1a/Rab2 GTPases, or the SNAp
REceptor (SNARE) component syntaxin 5, all of which block the conventional trafficking pathway from the ER to the Golgi. Moreover, CFTR transport through the non-conventional pathway was
potently blocked by overexpression of the late endosomal
target-SNARE syntaxin 13, suggesting that recycling through a
late Golgi/endosomal system was a prerequisite for CFTR maturation. We
conclude that CFTR transport in the early secretory pathway can involve
a novel pathway between the ER and late Golgi/endosomal compartments
that may influence developmental expression of CFTR on the cell surface in polarized epithelial cells.
*
This work was supported by an NRSA post-doctoral fellowship
from the National Institutes of Health (to B. D. M.) and National Institutes of Health Grant DK 51870 (to J. R.). This is TSRI
manuscript 14614-CB.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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