Cargando…
Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis
The study of actin in regulated exocytosis has a long history with many different results in numerous systems. A major limitation on identifying precise mechanisms has been the paucity of experimental systems in which actin function has been directly assessed alongside granule content release at dis...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3160584/ https://www.ncbi.nlm.nih.gov/pubmed/21844207 http://dx.doi.org/10.1083/jcb.201011119 |
_version_ | 1782210570411311104 |
---|---|
author | Nightingale, Thomas D. White, Ian J. Doyle, Emily L. Turmaine, Mark Harrison-Lavoie, Kimberly J. Webb, Kathleen F. Cramer, Louise P. Cutler, Daniel F. |
author_facet | Nightingale, Thomas D. White, Ian J. Doyle, Emily L. Turmaine, Mark Harrison-Lavoie, Kimberly J. Webb, Kathleen F. Cramer, Louise P. Cutler, Daniel F. |
author_sort | Nightingale, Thomas D. |
collection | PubMed |
description | The study of actin in regulated exocytosis has a long history with many different results in numerous systems. A major limitation on identifying precise mechanisms has been the paucity of experimental systems in which actin function has been directly assessed alongside granule content release at distinct steps of exocytosis of a single secretory organelle with sufficient spatiotemporal resolution. Using dual-color confocal microscopy and correlative electron microscopy in human endothelial cells, we visually distinguished two sequential steps of secretagogue-stimulated exocytosis: fusion of individual secretory granules (Weibel–Palade bodies [WPBs]) and subsequent expulsion of von Willebrand factor (VWF) content. Based on our observations, we conclude that for fusion, WPBs are released from cellular sites of actin anchorage. However, once fused, a dynamic ring of actin filaments and myosin II forms around the granule, and actomyosin II contractility squeezes VWF content out into the extracellular environment. This study therefore demonstrates how discrete actin cytoskeleton functions within a single cellular system explain actin filament–based prevention and promotion of specific exocytic steps during regulated secretion. |
format | Online Article Text |
id | pubmed-3160584 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-31605842012-02-22 Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis Nightingale, Thomas D. White, Ian J. Doyle, Emily L. Turmaine, Mark Harrison-Lavoie, Kimberly J. Webb, Kathleen F. Cramer, Louise P. Cutler, Daniel F. J Cell Biol Research Articles The study of actin in regulated exocytosis has a long history with many different results in numerous systems. A major limitation on identifying precise mechanisms has been the paucity of experimental systems in which actin function has been directly assessed alongside granule content release at distinct steps of exocytosis of a single secretory organelle with sufficient spatiotemporal resolution. Using dual-color confocal microscopy and correlative electron microscopy in human endothelial cells, we visually distinguished two sequential steps of secretagogue-stimulated exocytosis: fusion of individual secretory granules (Weibel–Palade bodies [WPBs]) and subsequent expulsion of von Willebrand factor (VWF) content. Based on our observations, we conclude that for fusion, WPBs are released from cellular sites of actin anchorage. However, once fused, a dynamic ring of actin filaments and myosin II forms around the granule, and actomyosin II contractility squeezes VWF content out into the extracellular environment. This study therefore demonstrates how discrete actin cytoskeleton functions within a single cellular system explain actin filament–based prevention and promotion of specific exocytic steps during regulated secretion. The Rockefeller University Press 2011-08-22 /pmc/articles/PMC3160584/ /pubmed/21844207 http://dx.doi.org/10.1083/jcb.201011119 Text en © 2011 Nightingale et al. 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Nightingale, Thomas D. White, Ian J. Doyle, Emily L. Turmaine, Mark Harrison-Lavoie, Kimberly J. Webb, Kathleen F. Cramer, Louise P. Cutler, Daniel F. Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis |
title | Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis |
title_full | Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis |
title_fullStr | Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis |
title_full_unstemmed | Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis |
title_short | Actomyosin II contractility expels von Willebrand factor from Weibel–Palade bodies during exocytosis |
title_sort | actomyosin ii contractility expels von willebrand factor from weibel–palade bodies during exocytosis |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3160584/ https://www.ncbi.nlm.nih.gov/pubmed/21844207 http://dx.doi.org/10.1083/jcb.201011119 |
work_keys_str_mv | AT nightingalethomasd actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT whiteianj actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT doyleemilyl actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT turmainemark actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT harrisonlavoiekimberlyj actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT webbkathleenf actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT cramerlouisep actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis AT cutlerdanielf actomyosiniicontractilityexpelsvonwillebrandfactorfromweibelpaladebodiesduringexocytosis |