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

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.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-B858-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-EAF5-2
Genre: Journal Article

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 Creators:
Drees, L.1, Author              
Königsmann, T.1, Author              
Jaspers, M. H. J.1, Author              
Pflanz, R.2, Author              
Riedel, D.3, Author              
Schuh, R.1, Author              
Affiliations:
1Research Group of Molecular Organogenesis, MPI for biophysical chemistry, Max Planck Society, ou_578591              
2Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society, ou_578590              
3Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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 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.

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Language(s): eng - English
 Dates: 2019-01-02
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pgen.1007882
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Title: PLoS Genetics
Source Genre: Journal
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Pages: 29 Volume / Issue: 15 (1) Sequence Number: e1007882 Start / End Page: - Identifier: -