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An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells
Clathrin provides an external scaffold to form small 50–100-nm transport vesicles. In contrast, formation of much larger dense-cored secretory granules is driven by selective aggregation of internal cargo at the trans-Golgi network; the only known role of clathrin in dense-cored secretory granules f...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171491/ https://www.ncbi.nlm.nih.gov/pubmed/16087708 http://dx.doi.org/10.1083/jcb.200503054 |
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author | Lui-Roberts, Winnie W.Y. Collinson, Lucy M. Hewlett, Lindsay J. Michaux, Grégoire Cutler, Daniel F. |
author_facet | Lui-Roberts, Winnie W.Y. Collinson, Lucy M. Hewlett, Lindsay J. Michaux, Grégoire Cutler, Daniel F. |
author_sort | Lui-Roberts, Winnie W.Y. |
collection | PubMed |
description | Clathrin provides an external scaffold to form small 50–100-nm transport vesicles. In contrast, formation of much larger dense-cored secretory granules is driven by selective aggregation of internal cargo at the trans-Golgi network; the only known role of clathrin in dense-cored secretory granules formation is to remove missorted proteins by small, coated vesicles during maturation of these spherical organelles. The formation of Weibel-Palade bodies (WPBs) is also cargo driven, but these are cigar-shaped organelles up to 5 μm long. We hypothesized that a cytoplasmic coat might be required to make these very different structures, and we found that new and forming WPBs are extensively, sometimes completely, coated. Overexpression of an AP-180 truncation mutant that prevents clathrin coat formation or reduced AP-1 expression by small interfering RNA both block WPB formation. We propose that, in contrast to other secretory granules, cargo aggregation alone is not sufficient to form immature WPBs and that an external scaffold that contains AP-1 and clathrin is essential. |
format | Text |
id | pubmed-2171491 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21714912008-03-05 An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells Lui-Roberts, Winnie W.Y. Collinson, Lucy M. Hewlett, Lindsay J. Michaux, Grégoire Cutler, Daniel F. J Cell Biol Research Articles Clathrin provides an external scaffold to form small 50–100-nm transport vesicles. In contrast, formation of much larger dense-cored secretory granules is driven by selective aggregation of internal cargo at the trans-Golgi network; the only known role of clathrin in dense-cored secretory granules formation is to remove missorted proteins by small, coated vesicles during maturation of these spherical organelles. The formation of Weibel-Palade bodies (WPBs) is also cargo driven, but these are cigar-shaped organelles up to 5 μm long. We hypothesized that a cytoplasmic coat might be required to make these very different structures, and we found that new and forming WPBs are extensively, sometimes completely, coated. Overexpression of an AP-180 truncation mutant that prevents clathrin coat formation or reduced AP-1 expression by small interfering RNA both block WPB formation. We propose that, in contrast to other secretory granules, cargo aggregation alone is not sufficient to form immature WPBs and that an external scaffold that contains AP-1 and clathrin is essential. The Rockefeller University Press 2005-08-15 /pmc/articles/PMC2171491/ /pubmed/16087708 http://dx.doi.org/10.1083/jcb.200503054 Text en Copyright © 2005, 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 Lui-Roberts, Winnie W.Y. Collinson, Lucy M. Hewlett, Lindsay J. Michaux, Grégoire Cutler, Daniel F. An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells |
title | An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells |
title_full | An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells |
title_fullStr | An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells |
title_full_unstemmed | An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells |
title_short | An AP-1/clathrin coat plays a novel and essential role in forming the Weibel-Palade bodies of endothelial cells |
title_sort | ap-1/clathrin coat plays a novel and essential role in forming the weibel-palade bodies of endothelial cells |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171491/ https://www.ncbi.nlm.nih.gov/pubmed/16087708 http://dx.doi.org/10.1083/jcb.200503054 |
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