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J. Cell Biol.,
Volume 141, Number 3, May 4, 1998 611-623
-adaptin-coated Domains on Endosomal Tubules



* Medical Research Council Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, England;
and Human transferrin receptors (TR) and receptors for polymeric immunoglobulins (pIgR) expressed in polarized MDCK cells maintain steady-state,
asymmetric distributions on the separate basolateral and apical surfaces even though they are trafficking
continuously into and across these cells. The intracellular mechanisms required to maintain these asymmetric
distributions have not been located. Here we show that
TR and pIgR internalize from both surfaces to a common interconnected endosome compartment that includes tubules with buds coated with clathrin lattices.
These buds generate vesicles that carry TR to the basolateral border. The lattices contain
Department of Cancer Biology, The Salk Institute for Biological Studies, San Diego, California 92186-5800
-adaptin and are
dispersed by treatment with brefeldin A (BFA). Since
BFA treatment abrogates the vectorial trafficking of
TR in polarized MDCK cells, we propose that the
clathrin-coated domains of the endosome tubules contain the polarized sorting mechanism responsible for
their preferential basolateral distribution.
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