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Vesicles modulate an actin network for asymmetric spindle positioning

Actin networks drive many essential cellular processes, including cell migration, cytokinesis and tissue morphogenesis. But how cells organize and regulate dynamic actin networks that consist of long, unbranched actin filaments is only poorly understood. This study in mouse oocytes reveals that cell...

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Detalles Bibliográficos
Autores principales: Holubcová, Zuzana, Howard, Gillian, Schuh, Melina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3797517/
https://www.ncbi.nlm.nih.gov/pubmed/23873150
http://dx.doi.org/10.1038/ncb2802
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author Holubcová, Zuzana
Howard, Gillian
Schuh, Melina
author_facet Holubcová, Zuzana
Howard, Gillian
Schuh, Melina
author_sort Holubcová, Zuzana
collection PubMed
description Actin networks drive many essential cellular processes, including cell migration, cytokinesis and tissue morphogenesis. But how cells organize and regulate dynamic actin networks that consist of long, unbranched actin filaments is only poorly understood. This study in mouse oocytes reveals that cells can use vesicles as adaptable, motorized network nodes to regulate the dynamics and density of intracellular actin networks. In particular, Rab11a-positive vesicles drive the network dynamics in a myosin-Vb-dependent manner, and modulate the network density by sequestering and clustering the network’s actin nucleators. We also report a simple way by which networks of different densities can be generated, namely by adjusting the number and volume of vesicles in the cell. This vesicle-based mechanism of actin network modulation is essential for asymmetric positioning of the meiotic spindle in mouse oocytes, a vital step in the development of a fertilizable egg in mammals.
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spelling pubmed-37975172014-02-01 Vesicles modulate an actin network for asymmetric spindle positioning Holubcová, Zuzana Howard, Gillian Schuh, Melina Nat Cell Biol Article Actin networks drive many essential cellular processes, including cell migration, cytokinesis and tissue morphogenesis. But how cells organize and regulate dynamic actin networks that consist of long, unbranched actin filaments is only poorly understood. This study in mouse oocytes reveals that cells can use vesicles as adaptable, motorized network nodes to regulate the dynamics and density of intracellular actin networks. In particular, Rab11a-positive vesicles drive the network dynamics in a myosin-Vb-dependent manner, and modulate the network density by sequestering and clustering the network’s actin nucleators. We also report a simple way by which networks of different densities can be generated, namely by adjusting the number and volume of vesicles in the cell. This vesicle-based mechanism of actin network modulation is essential for asymmetric positioning of the meiotic spindle in mouse oocytes, a vital step in the development of a fertilizable egg in mammals. 2013-07-21 2013-08 /pmc/articles/PMC3797517/ /pubmed/23873150 http://dx.doi.org/10.1038/ncb2802 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Holubcová, Zuzana
Howard, Gillian
Schuh, Melina
Vesicles modulate an actin network for asymmetric spindle positioning
title Vesicles modulate an actin network for asymmetric spindle positioning
title_full Vesicles modulate an actin network for asymmetric spindle positioning
title_fullStr Vesicles modulate an actin network for asymmetric spindle positioning
title_full_unstemmed Vesicles modulate an actin network for asymmetric spindle positioning
title_short Vesicles modulate an actin network for asymmetric spindle positioning
title_sort vesicles modulate an actin network for asymmetric spindle positioning
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3797517/
https://www.ncbi.nlm.nih.gov/pubmed/23873150
http://dx.doi.org/10.1038/ncb2802
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