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Cell-matrix's Response to Mechanical Forces01:13

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A Simplified System for Evaluating Cell Mechanosensing and Durotaxis In Vitro
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Structurally governed cell mechanotransduction through multiscale modeling.

John Kang1, Kathleen M Puskar2, Allen J Ehrlicher3

  • 1Lane Center for Computational Biology, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

Scientific Reports
|February 28, 2015
PubMed
Summary
This summary is machine-generated.

Cells use actin networks for mechanotransduction, involving transmission, sensing, and response. A new model reveals a bandpass mechanism controlling molecular release, suggesting disordered actin networks enhance cellular response robustness.

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Area of Science:

  • Cellular Mechanobiology
  • Biophysics
  • Systems Biology

Background:

  • Mechanotransduction, the process by which cells convert mechanical stimuli into biochemical signals, is crucial for cellular function.
  • Existing models often separate mechanotransduction into distinct phases: mechanotransmission, mechanosensing, and mechanoresponse.
  • The molecular mechanisms underlying how cells integrate these phases using shared structural components remain incompletely understood.

Purpose of the Study:

  • To develop a multiscale model integrating the three phases of mechanotransduction: mechanotransmission, mechanosensing, and mechanoresponse.
  • To investigate the role of actin filament networks and associated proteins in cellular mechanical responses.
  • To elucidate the specific mechanisms governing mechanically-induced molecular release from protein crosslinks.

Main Methods:

  • Development of a discrete multiscale model of actin filament networks incorporating geometric relaxation in response to stretching.
  • Assessment of three potential activating mechanisms at mechanosensitive crosslinks using a mixture model of molecular release.
  • Benchmarking model predictions against experimental data of mechanically-induced Rho GTPase FilGAP release from actin-filamin crosslinks.

Main Results:

  • The filamin-FilGAP mechanotransduction response is best explained by a bandpass mechanism, where molecular release is favored outside a specific range of crosslinking angles.
  • The model successfully links mechanical stretching to molecular release dynamics at the crosslink level.
  • A more disordered actin network structure enhances the cell's ability to finely tune molecular release, leading to a more robust mechanotransduction response.

Conclusions:

  • The study provides a unified model bridging molecular and systems-level understandings of mechanotransduction.
  • A bandpass mechanism at actin-filamin crosslinks regulates FilGAP release, demonstrating a specific molecular basis for mechanosensing.
  • Disordered actin networks offer a mechanism for enhanced cellular control and robustness in mechanotransduction.