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Transforming growth factor-beta (TGF-β) activation involves integrin binding and force. Structural analysis reveals how the prodomain shields TGF-β, requiring mechanical force to release the growth factor.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Transforming growth factor-beta (TGF-β) is crucial for cell growth and homeostasis.
  • TGF-β is stored in the extracellular matrix as a latent complex with its prodomain.
  • Activation requires integrin binding and mechanical force.

Purpose of the Study:

  • To elucidate the structural basis of latent TGF-β complex formation and activation.
  • To understand the role of the prodomain in regulating TGF-β availability.

Main Methods:

  • X-ray crystallography of dimeric porcine proTGF-β1.
  • Analysis of protein structure and interactions.

Main Results:

  • Revealed a novel ring-shaped prodomain fold shielding the growth factor.
  • Demonstrated that integrin binding alone is insufficient for TGF-β release.
  • Identified a force-dependent mechanism involving unfastening of a prodomain 'straitjacket'.

Conclusions:

  • The prodomain's structure is key to regulating TGF-β activity.
  • Force-dependent activation is essential for releasing active TGF-β.
  • Insights into TGF-β regulation have implications for development and disease.