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J. Biol. Chem., Vol. 277, Issue 9, 6858-6863, March 1, 2002
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From the Enteropeptidase, a type II transmembrane protein
of the enterocyte brush border, is sorted directly to the apical
membrane of Madin-Darby canine kidney II cells. Apical targeting
appears to be mediated by an N-terminal segment that contains a
27-amino acid residue O-glycosylated mucin-like domain
consisting of two short mucin-like repeats, A and B. Targeting signals
within these repeats were characterized by using green fluorescent
protein (GFP) as a reporter. Constructs with a cleavable signal peptide and both repeats A and B were secreted apically. Similar constructs lacking mucin repeats were secreted randomly. Either repeat A or B was
sufficient to direct apical targeting of GFP. O-linked oligosaccharides alone were not sufficient for targeting because fusion
to a different O-glycosylated motif did not alter the
random secretion of GFP, and several constructs with mutations in
either repeat A or B were O-glycosylated and secreted
randomly. In addition, repeat B appears to contain an apical targeting
signal that functions in the absence of glycosylation. Density
gradient centrifugation indicated that, unlike several other apically
targeted membrane and soluble proteins, apical sorting of mucin-GFP
chimeric proteins does not appear to utilize lipid rafts.
Mucin-like Domain of Enteropeptidase Directs Apical Targeting in
Madin-Darby Canine Kidney Cells*
and Department of Pathology and Immunology and
the § Howard Hughes Medical Institute, Departments of
Medicine and Biochemistry and Molecular Biophysics, Washington
University School of Medicine, St. Louis, Missouri 63110
*
This work was supported in part by National Institutes of
Health Grant DK50053.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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