Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed
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 tr...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2008
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| In: |
The journal of cell biology
Year: 2008, Volume: 183, Issue: 6, Pages: 999-1005 |
| ISSN: | 1540-8140 |
| DOI: | 10.1083/jcb.200810060 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1083/jcb.200810060 Verlag, kostenfrei, Volltext: http://jcb.rupress.org/content/183/6/999 
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| Author Notes: | Margaret L. Gardel, Benedikt Sabass, Lin Ji, Gaudenz Danuser, Ulrich S. Schwarz, and Clare M. Waterman |
| Summary: | 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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| Item Description: | Gesehen am 08.12.2017 |
| Physical Description: | Online Resource |
| ISSN: | 1540-8140 |
| DOI: | 10.1083/jcb.200810060 |