Journal
JOURNAL OF CELL BIOLOGY
Volume 202, Issue 1, Pages 163-177Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201303129
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Funding
- NHLBI Division of Intramural Research
- NHLBI [PO1 HL 46345]
- National Institutes of Health [T32GM008570]
- National Institute of General Medical Sciences (NIGMS) [RO1GM080568]
- NIGMS [U01 GM067230]
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In migrating cells, integrin-based focal adhesions (FAs) assemble in protruding lamellipodia in association with rapid filamentous actin (F-actin) assembly and retrograde flow. How dynamic F-actin is coupled to FA is not known. We analyzed the role of vinculin in integrating F-actin and FA dynamics by vinculin gene disruption in primary fibroblasts. Vinculin slowed F-actin flow in maturing FA to establish a lamellipodium-lamellum border and generate high extracellular matrix (ECM) traction forces. In addition, vinculin promoted nascent FA formation and turnover in lamellipodia and inhibited the frequency and rate of FA maturation. Characterization of a vinculin point mutant that specifically disrupts F-actin binding showed that vinculin-F-actin interaction is critical for these functions. However, FA growth rate correlated with F-actin flow speed independently of vinculin. Thus, vinculin functions as a molecular clutch, organizing leading edge F-actin, generating ECM traction, and promoting FA formation and turnover, but vinculin is dispensible for FA growth.
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