A C. elegans Zona Pellucida domain protein functions via its ZPc domain

Autoři: Jennifer D. Cohen aff001;  Jessica G. Bermudez aff002;  Matthew C. Good aff002;  Meera V. Sundaram aff001
Působiště autorů: Department of Genetics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, United States of America aff001;  Department of Bioengineering, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America aff002;  Department of Cell and Developmental Biology, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, United States of America aff003
Vyšlo v časopise: A C. elegans Zona Pellucida domain protein functions via its ZPc domain. PLoS Genet 16(11): e1009188. doi:10.1371/journal.pgen.1009188
Kategorie: Research Article
doi: 10.1371/journal.pgen.1009188


Zona Pellucida domain (ZP) proteins are critical components of the body’s external-most protective layers, apical extracellular matrices (aECMs). Although their loss or dysfunction is associated with many diseases, it remains unclear how ZP proteins assemble in aECMs. Current models suggest that ZP proteins polymerize via their ZPn subdomains, while ZPc subdomains modulate ZPn behavior. Using the model organism C. elegans, we investigated the aECM assembly of one ZP protein, LET-653, which shapes several tubes. Contrary to prevailing models, we find that LET-653 localizes and functions via its ZPc domain. Furthermore, we show that ZPc domain function requires cleavage at the LET-653 C-terminus, likely in part to relieve inhibition of the ZPc by the ZPn domain, but also to promote some other aspect of ZPc domain function. In vitro, the ZPc, but not ZPn, domain bound crystalline aggregates. These data offer a new model for ZP function whereby the ZPc domain is primarily responsible for matrix incorporation and tissue shaping.

Klíčová slova:

Caenorhabditis elegans – Extracellular matrix – Extracellular matrix proteins – Fluorescence imaging – Fluorescence recovery after photobleaching – Polymerization – Transfection – Vulva


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