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A more recent version of this article appeared on January 1, 2002
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Submitted on July 2, 2001
Revised on October 1, 2001
Accepted on October 26, 2001
1 Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, Connecticut
2 Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, Connecticut (present address: Institute of Biochemistry, ETH-Zentrum CHN, Universitatsstr. 16, 8092 Zurich, Switzerland
* Corresponding author. E-mail address: ira.mellman{at}yale.edu.
Mammalian epithelial cell plasma membrane domains are separated by junctional complexes supported by actin. The extent to which actin acts elsewhere to maintain cell polarity remains poorly understood. Using latrunculin B (Lat B) to depolymerize actin filaments, several basolateral plasma membrane proteins were found to lose their polarized distribution. This loss of polarity did not reflect lateral diffusion through junctional complexes since an LDL receptor mutant lacking a functional endocytosis signal remained basolateral after Lat B treatment. Furthermore Lat B treatment did not facilitate membrane diffusion across the tight junction as observed with EDTA or DMSO treatment. Detailed analysis of transferrin recycling confirmed Lat B depolarized recycling of transferrin from endosomes to the basolateral surface. Kinetic analysis suggested sorting was compromised at both basolateral early endosomes and perinuclear recycling endosomes. Despite loss of function, these two endosome populations remained distinct from each other and from early endosomes labeled by apically internalized ligand. Furthermore, apical and basolateral early endosomes were functionally distinct populations which directed traffic to a single common recycling endosomal compartment even after Lat B treatment. Thus, filamentous actin may help to guide receptor traffic from endosomes to the basolateral plasma membrane.
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