apple-itunes-app: app-id=409367154 prism.endingPage: 947 citation_title: Vesicles modulate an actin network for asymmetric spindle positioning WT.cg_s: Article access: Yes keywords: Meiosis, Actin, Membrane trafficking emanating: 134X76X223X157 citation_publisher: Nature Publishing Group citation_journal_title: Nature Cell Biology description: In mouse oocytes, Rab11a-positive vesicles are associated with actin nucleators. Schuh and colleagues find that these vesicles function as storage reservoirs for actin nucleators, that the actin network can be modulated by altering the number of Rab11a vesicles, and that actin dynamics affect the positioning of the meiotic spindle. WT.site_id: 18696 citation_date: 2013-08-01 title: The spindle is trapped in a static actin network if the function of Rab11a-positive vesicles is blocked. : Vesicles modulate an actin network for asymmetric spindle positioning : Nature Cell Biology : Nature Publishing Group DC.title: Vesicles modulate an actin network for asymmetric spindle positioning DC.date: 2013-07-21 prism.issn: 1465-7392 DC.publisher: Nature Publishing Group citation_online_date: 2013-07-21 WT.cg_n: Nature Cell Biology DC.creator: Zuzana Holubcová prism.issue: 8 DC.identifier: doi:10.1038/ncb2802 dc:title: The spindle is trapped in a static actin network if the function of Rab11a-positive vesicles is blocked. : Vesicles modulate an actin network for asymmetric spindle positioning : Nature Cell Biology : Nature Publishing Group Content-Encoding: UTF-8 prism.publicationDate: 2013-07-21 robots: noarchive DC.rights: © 2013 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. Content-Type: text/html; charset=UTF-8 citation_fulltext_world_readable: X-Parsed-By: org.apache.tika.parser.DefaultParser prism.rightsAgent: permissions@nature.com citation_author: Zuzana Holubcová citation_issue: 8 prism.eIssn: 1476-4679 X-UA-Compatible: IE=edge DC.language: en prism.volume: 15 citation_firstpage: 937 prism.startingPage: 937 WT.template: C viewport: width=device-width, initial-scale=1, maximum-scale=2.5 prism.publicationName: Nature Cell Biology citation_doi: doi:10.1038/ncb2802 prism.section: Article citation_volume: 15 WT.site_id_name: Max Planck Inst for Biophysical Chemistry (Karl Friedrich Bonhoeffer Inst) Content-Language: en prism.copyright: © 2013 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.