Traction stress in focal adhesions correlates biphasically with actin retrograde fl ow speed

Margaret L. Gardel, Benedikt Sabass, Lin Ji, Gaudenz Danuser, Ulrich S. Schwarz, Clare M. Waterman

Research output: Contribution to journalArticle

269 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)999-1005
Number of pages7
JournalJournal of Cell Biology
Volume183
Issue number6
DOIs
StatePublished - Dec 15 2008

Fingerprint

Focal Adhesions
Traction
Actins
Cell Movement
Myosin Type II
Guanosine
Extracellular Matrix
Microscopy

ASJC Scopus subject areas

  • Cell Biology
  • Medicine(all)

Cite this

Traction stress in focal adhesions correlates biphasically with actin retrograde fl ow speed. / Gardel, Margaret L.; Sabass, Benedikt; Ji, Lin; Danuser, Gaudenz; Schwarz, Ulrich S.; Waterman, Clare M.

In: Journal of Cell Biology, Vol. 183, No. 6, 15.12.2008, p. 999-1005.

Research output: Contribution to journalArticle

Gardel, Margaret L. ; Sabass, Benedikt ; Ji, Lin ; Danuser, Gaudenz ; Schwarz, Ulrich S. ; Waterman, Clare M. / Traction stress in focal adhesions correlates biphasically with actin retrograde fl ow speed. In: Journal of Cell Biology. 2008 ; Vol. 183, No. 6. pp. 999-1005.
@article{35cc779cc0944fd5bd0c63e1bb77b57a,
title = "Traction stress in focal adhesions correlates biphasically with actin retrograde fl ow speed",
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.",
author = "Gardel, {Margaret L.} and Benedikt Sabass and Lin Ji and Gaudenz Danuser and Schwarz, {Ulrich S.} and Waterman, {Clare M.}",
year = "2008",
month = "12",
day = "15",
doi = "10.1083/jcb.200810060",
language = "English (US)",
volume = "183",
pages = "999--1005",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "6",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=58249086114&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=58249086114&partnerID=8YFLogxK

U2 - 10.1083/jcb.200810060

DO - 10.1083/jcb.200810060

M3 - Article

C2 - 19075110

AN - SCOPUS:58249086114

VL - 183

SP - 999

EP - 1005

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 6

ER -