Abstract
How focal adhesions (FAs) convert retrograde fi lamentous actin (F-actin) fl ow into traction stress on the extracellular matrix to drive cell migration is unknown. Using combined traction force and fl uorescent 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. © 2008 Gardel et al.
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CITATION STYLE
Gardel, M. L., Sabass, B., Ji, L., Danuser, G., Schwarz, U. S., & Waterman, C. M. (2008). Traction stress in focal adhesions correlates biphasically with actin retrograde fl ow speed. Journal of Cell Biology, 183(6), 999–1005. https://doi.org/10.1083/jcb.200810060
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