Document Detail

Plectin deposition at podosome rings requires myosin contractility.
MedLine Citation:
PMID:  18553359     Owner:  NLM     Status:  MEDLINE    
Metalloproteinase-dependent tissue invasion requires the formation of podosomes and invadopodia for localized matrix degradation. Actin cytoskeleton remodeling via Arp2/3-mediated actin polymerization is essential for podosome formation, and dynamic microtubules have an important role in maintaining podosome turnover in macrophages and osteoclasts. Little is known, however, about the involvement of the intermediate filament cytoskeleton in formation, stabilization, and turnover of podosomes. Here we show that vimentin intermediate filaments colocalize with the early sites of podosome formation at the stress fiber - focal adhesion interface in cultured vascular smooth muscle cells, but do not directly contribute to podosome formation, or stabilization. In unstimulated A7r5 cells the cytolinker protein plectin poorly colocalized with vimentin and the microdomains, but following induction by phorbol ester accumulated in the rings that surround the podosomes. In plectin-deficient A7r5 cells actin stress fiber remodelling is reduced in response to PDBu, and small podosomes remain localized at stable actin stress fibres. Pharmacological inhibition of actomyosin contractility by blebbistatin leads to an aberrant localization of podosomes away from the cell periphery and induces failure of plectin to surround the outer perimeter of these invasive adhesions. Taken together, we conclude that plectin is involved in growth and maturation of podosomes by reducing focal adhesion and stress fiber turnover, and that actomyosin-dependent contractility is required for the peripheral localization and specific deposition of plectin at the podosome rings.
Annica Gad; Sibylle Lach; Luca Crimaldi; Mario Gimona
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell motility and the cytoskeleton     Volume:  65     ISSN:  1097-0169     ISO Abbreviation:  Cell Motil. Cytoskeleton     Publication Date:  2008 Aug 
Date Detail:
Created Date:  2008-07-21     Completed Date:  2008-12-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8605339     Medline TA:  Cell Motil Cytoskeleton     Country:  United States    
Other Details:
Languages:  eng     Pagination:  614-25     Citation Subset:  IM    
Copyright Information:
(c) 2008 Wiley-Liss, Inc.
Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Via Nazionale 8a, I-66030 Santa Maria Imbaro, Italy.
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MeSH Terms
Actins / metabolism
Blotting, Western
Cell Line
Cell Movement / drug effects,  physiology
Cytoskeleton / drug effects,  metabolism
Focal Adhesions / metabolism
Heterocyclic Compounds with 4 or More Rings / pharmacology
Intermediate Filaments / metabolism
Microscopy, Fluorescence
Muscle, Smooth / cytology,  drug effects,  metabolism
Myosins / metabolism*,  physiology
Phorbol 12,13-Dibutyrate / pharmacology
Plectin / genetics,  metabolism*
Pseudopodia / drug effects,  metabolism*,  physiology
RNA Interference
Vimentin / metabolism
Reg. No./Substance:
0/Actins; 0/Heterocyclic Compounds with 4 or More Rings; 0/Plectin; 0/Vimentin; 0/blebbistatin; 37558-16-0/Phorbol 12,13-Dibutyrate; EC

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

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