Document Detail

Dimensional and temporal controls of three-dimensional cell migration by zyxin and binding partners.
MedLine Citation:
PMID:  22395610     Owner:  NLM     Status:  MEDLINE    
Spontaneous molecular oscillations are ubiquitous in biology. But to our knowledge, periodic cell migratory patterns have not been observed. Here we report the highly regular, periodic migration of cells along rectilinear tracks generated inside three-dimensional matrices, with each excursion encompassing several cell lengths, a phenotype that does not occur on conventional substrates. Short hairpin RNA depletion shows that these one-dimensional oscillations are uniquely controlled by zyxin and binding partners α-actinin and p130Cas, but not vasodilator-stimulated phosphoprotein and cysteine-rich protein 1. Oscillations are recapitulated for cells migrating along one-dimensional micropatterns, but not on two-dimensional compliant substrates. These results indicate that although two-dimensional motility can be well described by speed and persistence, three-dimensional motility requires two additional parameters, the dimensionality of the cell paths in the matrix and the temporal control of cell movements along these paths. These results also suggest that the zyxin/α-actinin/p130Cas module may ensure that motile cells in a three-dimensional matrix explore the largest space possible in minimum time.
Stephanie I Fraley; Yunfeng Feng; Anjil Giri; Gregory D Longmore; Denis Wirtz
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-03-06
Journal Detail:
Title:  Nature communications     Volume:  3     ISSN:  2041-1723     ISO Abbreviation:  Nat Commun     Publication Date:  2012  
Date Detail:
Created Date:  2012-03-07     Completed Date:  2012-08-02     Revised Date:  2013-06-25    
Medline Journal Info:
Nlm Unique ID:  101528555     Medline TA:  Nat Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  719     Citation Subset:  IM    
Department of Chemical and Biomolecular Engineering, The Johns Hopkins University, 3400 N Charles Street, Maryland Hall Room 223, Baltimore, Maryland 21218, USA.
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MeSH Terms
Actinin / metabolism*
Carrier Proteins / metabolism
Cell Adhesion Molecules / metabolism
Cell Line, Tumor
Cell Movement*
Crk-Associated Substrate Protein / metabolism*
Focal Adhesions / metabolism
LIM Domain Proteins / metabolism
Microfilament Proteins / metabolism
Phosphoproteins / metabolism
RNA Interference
RNA, Small Interfering
Zyxin / metabolism*
Grant Support
Reg. No./Substance:
0/BCAR1 protein, human; 0/CRIP1 protein, human; 0/Carrier Proteins; 0/Cell Adhesion Molecules; 0/Crk-Associated Substrate Protein; 0/LIM Domain Proteins; 0/Microfilament Proteins; 0/Phosphoproteins; 0/RNA, Small Interfering; 0/Zyxin; 0/vasodilator-stimulated phosphoprotein; 11003-00-2/Actinin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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