Conserved function of the matriptase-prostasin proteolytic cascade during epithelial morphogenesis.
Animals
Carrier Proteins
/ genetics
Cell Differentiation
/ genetics
Chitin
/ genetics
Drosophila Proteins
/ genetics
Drosophila melanogaster
/ genetics
Endopeptidases
/ genetics
Epithelial Cells
/ metabolism
Epithelium
/ growth & development
Extracellular Matrix
/ genetics
Extracellular Matrix Proteins
/ genetics
Humans
Morphogenesis
/ genetics
Protein Domains
/ genetics
Serine Endopeptidases
/ genetics
Signal Transduction
Journal
PLoS genetics
ISSN: 1553-7404
Titre abrégé: PLoS Genet
Pays: United States
ID NLM: 101239074
Informations de publication
Date de publication:
01 2019
01 2019
Historique:
received:
10
10
2018
accepted:
06
12
2018
revised:
14
01
2019
pubmed:
3
1
2019
medline:
12
3
2019
entrez:
3
1
2019
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 30601807
doi: 10.1371/journal.pgen.1007882
pii: PGENETICS-D-18-01994
pmc: PMC6331135
doi:
Substances chimiques
Carrier Proteins
0
DPY protein, Drosophila
0
Drosophila Proteins
0
Extracellular Matrix Proteins
0
pio protein, Drosophila
0
Chitin
1398-61-4
Endopeptidases
EC 3.4.-
Serine Endopeptidases
EC 3.4.21.-
matriptase
EC 3.4.21.-
tpr protease
EC 3.4.99.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1007882Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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