English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons228875

Drees,  L.
Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons213639

Königsmann,  T.
Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons32558

Jaspers,  M. H. J.
Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15636

Pflanz,  R.
Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15710

Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15806

Schuh,  R.
Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)

3016898.pdf
(Publisher version), 7MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Drees, L., Königsmann, T., Jaspers, M. H. J., Pflanz, R., Riedel, D., & Schuh, R. (2019). Conserved function of the matriptase-prostasin proteolytic cascade during epithelial morphogenesis. PLoS Genetics, 15(1): e1007882. doi:10.1371/journal.pgen.1007882.


Cite as: http://hdl.handle.net/21.11116/0000-0002-B858-C
Abstract
Extracellular matrix (ECM) assembly and remodelling is critical during development and organ morphogenesis. Dysregulation of ECM is implicated in many pathogenic conditions, including cancer. The type II transmembrane serine protease matriptase and the serine protease prostasin are key factors in a proteolytic cascade that regulates epithelial ECM differentiation during development in vertebrates. Here, we show by rescue experiments that the Drosophila proteases Notopleural (Np) and Tracheal-prostasin (Tpr) are functional homologues of matriptase and prostasin, respectively. Np mediates morphogenesis and remodelling of apical ECM during tracheal system development and is essential for maintenance of the transepithelial barrier function. Both Np and Tpr degrade the zona pellucida-domain (ZP-domain) protein Dumpy, a component of the transient tracheal apical ECM. Furthermore, we demonstrate that Tpr zymogen and the ZP domain of the ECM protein Piopio are cleaved by Np and matriptase in vitro. Our data indicate that the evolutionarily conserved ZP domain, present in many ECM proteins of vertebrates and invertebrates, is a novel target of the conserved matriptase-prostasin proteolytic cascade.