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Conserved function of the matriptase-prostasin proteolytic cascade during epithelial morphogenesis.

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Drosophila proteases Notopleural (Np) and Tracheal-prostasin (Tpr) are functional homologues of vertebrate matriptase and prostasin. They regulate extracellular matrix (ECM) assembly and are key targets in conserved proteolytic cascades.

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Area of Science:

  • Developmental Biology
  • Protease biochemistry
  • Extracellular Matrix Biology

Background:

  • Extracellular matrix (ECM) assembly and remodeling are crucial for development and organogenesis.
  • Dysregulation of ECM is linked to various diseases, including cancer.
  • The matriptase-prostasin proteolytic cascade is vital for epithelial ECM differentiation in vertebrates.

Purpose of the Study:

  • To identify functional homologues of vertebrate matriptase and prostasin in Drosophila.
  • To investigate the roles of Drosophila proteases Np and Tpr in tracheal system development and ECM remodeling.
  • To elucidate the targets and regulation of the conserved matriptase-prostasin proteolytic cascade.

Main Methods:

  • Rescue experiments in Drosophila to validate protease function.
  • Analysis of Np and Tpr roles in tracheal system morphogenesis and barrier function.
  • In vitro cleavage assays using Drosophila ECM proteins and vertebrate proteases.

Main Results:

  • Drosophila Np and Tpr are functional homologues of matriptase and prostasin.
  • Np is essential for apical ECM remodeling and transepithelial barrier maintenance in the tracheal system.
  • Np and Tpr degrade the ZP-domain protein Dumpy; Np and matriptase cleave Tpr zymogen and the Piopio ZP domain.

Conclusions:

  • The conserved matriptase-prostasin cascade regulates ECM assembly and remodeling across species.
  • The zona pellucida (ZP) domain is a novel target of this conserved proteolytic cascade.
  • Understanding this cascade provides insights into ECM-related developmental processes and diseases.