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Vol. 11, Issue 6, 2131-2150, June 2000
Renal-Electrolyte Division of the Department of Medicine,
Laboratory of Epithelial Biology, and Department of Cell Biology and
Physiology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261
When fluid-phase markers are internalized from opposite poles of
polarized Madin-Darby canine kidney cells, they accumulate in distinct
apical and basolateral early endosomes before meeting in late
endosomes. Recent evidence suggests that significant mixing of apically
and basolaterally internalized membrane proteins occurs in specialized
apical endosomal compartments, including the common recycling endosome
and the apical recycling endosome (ARE). The relationship between these
latter compartments and the fluid-labeled apical early endosome is
unknown at present. We report that when the apical recycling marker,
membrane-bound immunoglobulin A (a ligand for the polymeric
immunoglobulin receptor), and fluid-phase dextran are cointernalized
from the apical poles of Madin-Darby canine kidney cells, they enter a
shared apical early endosome (
2.5 min at 37°C) and are then rapidly
segregated from one another. The dextran remains in the large
supranuclear EEA1-positive early endosomes while recycling polymeric
immunoglobulin receptor-bound immunoglobulin A is delivered to a
Rab11-positive subapical recycling compartment. This latter step
requires an intact microtubule cytoskeleton. Receptor-bound
transferrin, a marker of the basolateral recycling pathway, has limited
access to the fluid-rich apical early endosome but is excluded from the
subapical elements of the Rab11-positive recycling compartment. We
propose that the term ARE be used to describe the subapical
Rab11-positive compartment and that the ARE is distinct from both the
transferrin-rich common recycling endosome and the fluid-rich apical
early endosome.
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