Document Detail


Lamellipodial actin mechanically links myosin activity with adhesion-site formation.
MedLine Citation:
PMID:  17289574     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cell motility proceeds by cycles of edge protrusion, adhesion, and retraction. Whether these functions are coordinated by biochemical or biomechanical processes is unknown. We find that myosin II pulls the rear of the lamellipodial actin network, causing upward bending, edge retraction, and initiation of new adhesion sites. The network then separates from the edge and condenses over the myosin. Protrusion resumes as lamellipodial actin regenerates from the front and extends rearward until it reaches newly assembled myosin, initiating the next cycle. Upward bending, observed by evanescence and electron microscopy, results in ruffle formation when adhesion strength is low. Correlative fluorescence and electron microscopy shows that the regenerating lamellipodium forms a cohesive, separable layer of actin above the lamellum. Thus, actin polymerization periodically builds a mechanical link, the lamellipodium, connecting myosin motors with the initiation of adhesion sites, suggesting that the major functions driving motility are coordinated by a biomechanical process.
Authors:
Grégory Giannone; Benjamin J Dubin-Thaler; Olivier Rossier; Yunfei Cai; Oleg Chaga; Guoying Jiang; William Beaver; Hans-Günther Döbereiner; Yoav Freund; Gary Borisy; Michael P Sheetz
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Cell     Volume:  128     ISSN:  0092-8674     ISO Abbreviation:  Cell     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-02-09     Completed Date:  2007-03-28     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  561-75     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism*
Animals
Cell Adhesion*
Cell Movement
Fibroblasts / cytology
Mice
Microscopy, Electron
Microscopy, Fluorescence
Myosin Type II / genetics,  metabolism
Myosins / metabolism*
Periodicity
Polymers / metabolism
Pseudopodia / chemistry*,  ultrastructure
Grant Support
ID/Acronym/Agency:
PN1 EY016586/EY/NEI NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 0/Polymers; EC 3.6.1.-/Myosin Type II; EC 3.6.4.1/Myosins

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