TY - JOUR
T1 - Traction stress in focal adhesions correlates biphasically with actin retrograde fl ow speed
AU - Gardel, Margaret L.
AU - Sabass, Benedikt
AU - Ji, Lin
AU - Danuser, Gaudenz
AU - Schwarz, Ulrich S.
AU - Waterman, Clare M.
PY - 2008/12/15
Y1 - 2008/12/15
N2 - 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.
AB - 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.
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U2 - 10.1083/jcb.200810060
DO - 10.1083/jcb.200810060
M3 - Article
C2 - 19075110
AN - SCOPUS:58249086114
SN - 0021-9525
VL - 183
SP - 999
EP - 1005
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 6
ER -