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Related Experiment Videos

Force transduction by Triton cytoskeletons.

Yasuhiro Sawada1, Michael P Sheetz

  • 1Department of Biological Sciences, Columbia University, New York, NY 10027, USA.

The Journal of Cell Biology
|February 13, 2002
PubMed
Summary

Cellular matrix forces trigger signal transduction through cytoskeletal protein binding changes. This study reveals stretch-dependent alterations in cytoplasmic protein interactions within the cytoskeleton, impacting cellular responses.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Mechanobiology

Background:

  • Force-initiated signal transduction is crucial for cellular function.
  • Mechanisms involve ionic channels or cytoskeletal-matrix interactions.

Purpose of the Study:

  • Investigate stretch-dependent binding of cytoplasmic proteins to cell cytoskeletons.
  • Elucidate the role of cytoskeletal protein conformation in force transduction.

Main Methods:

  • Stretching Triton X-100-insoluble L-929 cell cytoskeletons by 10%.
  • Incubating stretched cytoskeletons with biotinylated cytoplasmic proteins.
  • Analyzing protein binding using 2D gel electrophoresis and photocleavable biotin tags.

Main Results:

  • Over 10 cytoplasmic protein spots showed stretch-dependent binding.
  • Paxillin, focal adhesion kinase, and p130Cas binding increased with stretch.
  • Vinculin binding remained unchanged, while actin binding decreased.

Conclusions:

  • Force transduction involves force-dependent conformational changes in the integrated cytoskeleton.
  • Paxillin's stretch-dependent binding is conserved in vitro and in vivo.
  • Cytoskeletal protein dynamics are key to sensing and responding to mechanical forces.

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