Document Detail

The Functional Antagonism between Eg5 and Dynein in Spindle Bipolarization Is Not Compatible with a Simple Push-Pull Model.
MedLine Citation:
PMID:  22832270     Owner:  NLM     Status:  In-Data-Review    
During cell division, the molecular motor Eg5 crosslinks overlapping antiparallel microtubules and pushes them apart to separate mitotic spindle poles. Dynein has been proposed as a direct antagonist of Eg5 at the spindle equator, pulling on antiparallel microtubules and favoring spindle collapse. Some of the experiments supporting this hypothesis relied on endpoint quantifications of spindle phenotypes rather than following individual cell fates over time. Here, we present a mathematical model and proof-of-principle experiments to demonstrate that endpoint quantifications can be fundamentally misleading because they overestimate defective phenotypes. Indeed, live-cell imaging reveals that, while depletion of dynein or the dynein binding protein Lis1 enables spindle formation in presence of an Eg5 inhibitor, the activities of dynein and Eg5 cannot be titrated against each other. Thus, dynein most likely antagonizes Eg5 indirectly by exerting force at different spindle locations rather than through a simple push-pull mechanism at the spindle equator.
Stefan Florian; Thomas U Mayer
Publication Detail:
Type:  Journal Article     Date:  2012-04-20
Journal Detail:
Title:  Cell reports     Volume:  1     ISSN:  2211-1247     ISO Abbreviation:  Cell Rep     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-07-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101573691     Medline TA:  Cell Rep     Country:  United States    
Other Details:
Languages:  eng     Pagination:  408-16     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 The Authors. Published by Elsevier Inc. All rights reserved.
Department of Biology and Konstanz Research School Chemical Biology, University of Konstanz, Universitätsstrasse 10, 78457 Konstanz, Germany.
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