Document Detail


A microtubule-binding myosin required for nuclear anchoring and spindle assembly.
MedLine Citation:
PMID:  15372037     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proper spindle positioning and orientation are essential for asymmetric cell division and require microtubule-actin filament (F-actin) interactions in many systems. Such interactions are particularly important in meiosis, where they mediate nuclear anchoring, as well as meiotic spindle assembly and rotation, two processes required for asymmetric cell division. Myosin-10 proteins are phosphoinositide-binding, actin-based motors that contain carboxy-terminal MyTH4 and FERM domains of unknown function. Here we show that Xenopus laevis myosin-10 (Myo10) associates with microtubules in vitro and in vivo, and is concentrated at the point where the meiotic spindle contacts the F-actin-rich cortex. Microtubule association is mediated by the MyTH4-FERM domains, which bind directly to purified microtubules. Disruption of Myo10 function disrupts nuclear anchoring, spindle assembly and spindle-F-actin association. Thus, this myosin has a novel and critically important role during meiosis in integrating the F-actin and microtubule cytoskeletons.
Authors:
Kari L Weber; Anna M Sokac; Jonathan S Berg; Richard E Cheney; William M Bement
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Nature     Volume:  431     ISSN:  1476-4687     ISO Abbreviation:  Nature     Publication Date:  2004 Sep 
Date Detail:
Created Date:  2004-09-16     Completed Date:  2004-10-15     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  325-9     Citation Subset:  IM    
Affiliation:
Department of Zoology, University of Wisconsin, Madison, Madison, Wisconsin 53706, USA.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism
Animals
Cell Nucleus / chemistry,  metabolism*
Meiosis / physiology*
Microtubules / chemistry,  metabolism*
Mitotic Spindle Apparatus / chemistry*,  metabolism*
Myosins / chemistry,  metabolism*
Protein Binding
Protein Structure, Tertiary
Xenopus Proteins / chemistry,  metabolism*
Xenopus laevis
Chemical
Reg. No./Substance:
0/Actins; 0/Myo10 protein, Xenopus; 0/Xenopus Proteins; EC 3.6.4.1/Myosins
Comments/Corrections
Comment In:
Nature. 2004 Sep 16;431(7006):252-3   [PMID:  15372012 ]

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