Document Detail

Intact vinculin protein is required for control of cell shape, cell mechanics, and rac-dependent lamellipodia formation.
MedLine Citation:
PMID:  11785963     Owner:  NLM     Status:  MEDLINE    
Studies were carried out using vinculin-deficient F9 embryonic carcinoma (gamma229) cells to analyze the relationship between structure and function within the focal adhesion protein vinculin, in the context of control of cell shape, cell mechanics, and movement. Atomic force microscopy studies revealed that transfection of the head (aa 1-821) or tail (aa 811-1066) domain of vinculin, alone or together, was unable to fully reverse the decrease in cell stiffness, spreading, and lamellipodia formation caused by vinculin deficiency. In contrast, replacement with intact vinculin completely restored normal cell mechanics and spreading regardless of whether its tyrosine phosphorylation site was deleted. Constitutively active rac also only induced extension of lamellipodia when microinjected into cells that expressed intact vinculin protein. These data indicate that vinculin's ability to physically couple integrins to the cytoskeleton, to mechanically stabilize cell shape, and to support rac-dependent lamellipodia formation all appear to depend on its intact three-dimensional structure.
Wolfgang H Goldmann; Donald E Ingber
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  290     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2002 Jan 
Date Detail:
Created Date:  2002-01-11     Completed Date:  2002-02-11     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  749-55     Citation Subset:  IM; S    
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
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MeSH Terms
Binding Sites / physiology
Cell Adhesion / drug effects,  physiology
Cell Line
Cell Membrane / drug effects,  metabolism,  ultrastructure
Cell Size / drug effects,  physiology
Neoplastic Stem Cells / cytology*,  metabolism*,  ultrastructure
Pseudopodia / drug effects,  metabolism*,  ultrastructure
Vinculin / deficiency,  genetics,  metabolism*
rac GTP-Binding Proteins / administration & dosage,  metabolism*
Grant Support
Reg. No./Substance:
125361-02-6/Vinculin; EC GTP-Binding Proteins
D E Ingber / Harvard Med Sch, Boston, MA

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

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