Recycling Endosomes Can Serve as Intermediates during Transport from the Golgi to the Plasma Membrane of MDCK Cells

The AP-1B clathrin adaptor complex is responsible for the polarized transport of many basolateral membrane proteins in epithelial cells. Localization of AP-1B to recycling endosomes (REs) along with other components (exocyst subunits and Rab8) involved in AP-1B-dependent transport suggested that RE...

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Bibliographic Details
Published in:The Journal of cell biology 2004-11, Vol.167 (3), p.531-543
Main Authors: Ang, Agnes Lee, Taguchi, Tomohiko, Francis, Stephen, Fölsch, Heike, Murrells, Lindsay J., Pypaert, Marc, Warren, Graham, Mellman, Ira
Format: Article
Language:English
Subjects:
Adaptor Protein Complex 1 - metabolism
Animals
Cell adhesion & migration
Cell Line
Cell Membrane - metabolism
Cell membranes
CHO cells
Dogs
Endocytosis
Endosomes
Endosomes - physiology
Epithelial cells
Freight
Golgi apparatus
Golgi Apparatus - metabolism
Hepatocytes
Kidney cells
Membrane Glycoproteins - metabolism
Membranes
Microscopy
Microscopy, Fluorescence
Microscopy, Video
Protein Transport
Proteins
Recycling
Transferrin
Vesicular stomatitis virus
Viral Envelope Proteins - metabolism
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Summary:The AP-1B clathrin adaptor complex is responsible for the polarized transport of many basolateral membrane proteins in epithelial cells. Localization of AP-1B to recycling endosomes (REs) along with other components (exocyst subunits and Rab8) involved in AP-1B-dependent transport suggested that RE might be an intermediate between the Golgi and the plasma membrane. Although the involvement of endosomes in the secretory pathway has long been suspected, we now present direct evidence using four independent methods that REs play a role in basolateral transport in MDCK cells. Newly synthesized AP-1B-dependent cargo, vesicular stomatitis virus glycoprotein G (VSV-G), was found by video microscopy, immunoelectron microscopy, and cell fractionation to enter transferrin-positive REs within a few minutes after exit from the trans-Golgi network. Although transient, RE entry appears essential because enzymatic inactivation of REs blocked VSV-G delivery to the cell surface. Because an apically targeted VSV-G mutant behaved similarly, these results suggest that REs not only serve as an intermediate but also as a common site for polarized sorting on the endocytic and secretory pathways.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200408165