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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...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2004
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172492/ https://www.ncbi.nlm.nih.gov/pubmed/15534004 http://dx.doi.org/10.1083/jcb.200408165 |
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author | Ang, Agnes Lee Taguchi, Tomohiko Francis, Stephen Fölsch, Heike Murrells, Lindsay J. Pypaert, Marc Warren, Graham Mellman, Ira |
author_facet | Ang, Agnes Lee Taguchi, Tomohiko Francis, Stephen Fölsch, Heike Murrells, Lindsay J. Pypaert, Marc Warren, Graham Mellman, Ira |
author_sort | Ang, Agnes Lee |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2172492 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21724922008-03-05 Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells Ang, Agnes Lee Taguchi, Tomohiko Francis, Stephen Fölsch, Heike Murrells, Lindsay J. Pypaert, Marc Warren, Graham Mellman, Ira J Cell Biol Research Articles 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. The Rockefeller University Press 2004-11-08 /pmc/articles/PMC2172492/ /pubmed/15534004 http://dx.doi.org/10.1083/jcb.200408165 Text en Copyright © 2004, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Ang, Agnes Lee Taguchi, Tomohiko Francis, Stephen Fölsch, Heike Murrells, Lindsay J. Pypaert, Marc Warren, Graham Mellman, Ira Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells |
title | Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells |
title_full | Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells |
title_fullStr | Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells |
title_full_unstemmed | Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells |
title_short | Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells |
title_sort | recycling endosomes can serve as intermediates during transport from the golgi to the plasma membrane of mdck cells |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172492/ https://www.ncbi.nlm.nih.gov/pubmed/15534004 http://dx.doi.org/10.1083/jcb.200408165 |
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