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J Biol Chem, Vol. 274, Issue 53, 37551-37558, December 31, 1999
§,
,§§
From the Trafficking of the
Na+/H+ exchanger isoform 3 (NHE3) between
sub-apical vesicles and apical membrane of epithelial cells is a
suggested mechanism of regulation of NHE3 activity. When epitope-tagged NHE3 was stably expressed in NHE-deficient Chinese hamster ovary cells,
a sizable fraction was found in recycling endosomes. This system was
used to analyze the mechanism of endocytosis of NHE3. Immunofluorescence and radiolabeling experiments showed that inhibition of clathrin-mediated endocytosis using hypertonicity, acid treatment, or K+ depletion inhibited internalization of NHE3.
Moreover, transient transfection of an inhibitory mutant of dynamin
(DynS45N) blocked the clathrin-mediated uptake of transferrin, as well
as the endocytosis of NHE3. In ileal villus cells, endogenous NHE3 was
also found to co-purify with isolated clathrin-coated vesicles, thereby
confirming their association in native tissues. The role of COP-I
subunits in the intracellular traffic of NHE3 was evaluated using
ldlF cells, which bear a temperature-sensitive mutation in
the Division of Respiratory Medicine, Department
of Medicine, University of Toronto, Toronto, Ontario M5S 1A8, Canada,
the ¶ Division of Gastroenterology, The Johns Hopkins University
School of Medicine, Baltimore, Maryland 21205, the
§ Division of Cell Biology, Research Institute, The Hospital
for Sick Children, Toronto, Ontario M5G 1X8, Canada, and the
Department of Physiology, McGill
University, Montréal, Québec, H3G 1Y6, Canada
-COP subunit. At the permissive temperature, NHE3 distributed
normally, whereas at the restrictive temperature, which induces rapid
degradation of -COP, NHE3 was still internalized, but its
subcellular distribution was altered. These results indicate that
endocytosis of NHE3 occurs primarily via clathrin-coated pits and
vesicles and that normal intracellular trafficking of NHE3 involves an
-COP-dependent step.
Industry Research Scholar. Supported by the American Digestive
Health Foundation of the United States.
**
International Scholar of the Howard Hughes Medical Institute and is
the current holder of the Pitbaldo Chair in Cell Biology at the
Hospital for Sick Children. Cross-appointed to the Department of
Biochemistry, University of Toronto.
§§
Medical Research Council of Canada Scientist. To whom
correspondence should be addressed: Dept. of Physiology, McGill
University, McIntyre Medical Science Bldg., 3655 Drummond St.,
Montreal, Quebec H3G 1Y6, Canada. Tel.: 514-398-8335; Fax:
514-398-7452; E-mail: orlowski@med.mcgill.ca.
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