Document Detail

A force-dependent state controls the coordination of processive myosin V.
MedLine Citation:
PMID:  16150709     Owner:  NLM     Status:  MEDLINE    
Myosin V is an efficient processive molecular motor. Recent experiments have shown how the structure and kinetics of myosin V are specialized to produce a highly processive motor capable of taking multiple 36-nm steps on an actin filament track. Here, we examine how two identical heads coordinate their activity to produce efficient hand-over-hand stepping. We have used a modified laser-trap microscope to apply a approximately 2-pN forward or backward force on a single-headed myosin V molecule, hypothesized to simulate forces experienced by the rear or lead head, respectively. We found that pulling forward produces only a small change in the kinetics, whereas pulling backward induces a large reduction in the cycling of the head. These results support a model in which the coordination of myosin V stepping is mediated by strain-generated inhibition of the lead head.
Thomas J Purcell; H Lee Sweeney; James A Spudich
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Publication Detail:
Type:  Journal Article     Date:  2005-09-06
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  102     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2005 Sep 
Date Detail:
Created Date:  2005-09-28     Completed Date:  2005-11-21     Revised Date:  2014-03-19    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13873-8     Citation Subset:  IM    
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MeSH Terms
Microscopy, Confocal
Molecular Motor Proteins / genetics,  metabolism*,  ultrastructure*
Myosin Type V / genetics,  metabolism*,  ultrastructure*
Grant Support
Reg. No./Substance:
0/Molecular Motor Proteins; EC 3.6.1.-/Myosin Type V
Comment In:
Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13719-20   [PMID:  16172373 ]

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