Journal
JOURNAL OF CELL BIOLOGY
Volume 183, Issue 6, Pages 999-1005Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200810060
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Funding
- National Institutes of Health (NIH)/National Heart, Lung, and Blood Institute (C. M. Waterman)
- Burroughs Wellcome Fund Career Award at the Scientific Interface
- Jane Coffin Childs Fellowship
- NIH Director's Pioneer Award [DP10D00354]
- Center for Modelling and Simulation in the Biosciences at Heidelberg (U. S. Schwarz)
- [R01 GM71868]
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How focal adhesions (FAs) convert retrograde filamentous actin (F-actin) flow into traction stress on the extracellular matrix to drive cell migration is unknown. Using combined traction force and fluorescent speckle microscopy, we observed a robust biphasic relationship between F-actin speed and traction force. F-actin speed is inversely related to traction stress near the cell edge where FAs are formed and F-actin motion is rapid. In contrast, larger FAs where the F-actin speed is low are marked by a direct relationship between F-actin speed and traction stress. We found that the biphasic switch is determined by a threshold F-actin speed of 8-10 nm/s, independent of changes in FA protein density, age, stress magnitude, assembly/disassembly status, or subcellular position induced by pleiotropic perturbations to Rho family guanosine triphosphatase signaling and myosin II activity. Thus, F-actin speed is a fundamental regulator of traction force at FAs during cell migration.
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