ArticleBMC biochemistry2006
The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.
Article in BMC biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 82 citations in OpenAlex.
- Transcriptomic Analysis ofInternational journal of molecular sciences · 2026Article
- Transcriptomic Analysis ofbioRxiv : the preprint server for biology · 2026Article
- Fundamental and unique roles of PLAC1 in the regulation of rat and human trophoblast cell development.Development (Cambridge, England) · 2026Article
- CIROZ is dispensable in ancestral vertebrates but essential for left-right patterning in humans.American journal of human genetics · 2025Article
- Female fertility and the mammalian egg'sHistology and histopathology · 2024Review
- Diversification of von Willebrand Factor A and Chitin-Binding Domains in Pif/BMSPs Among Mollusks.Journal of molecular evolution · 2024Article
- Case report: A novel homozygous variant in ZP3 is associated with human empty follicle syndrome.Frontiers in genetics · 2023Article
- Evolution of Epidermal Growth Factor (EGF)-like and Zona Pellucida Domains Containing Shell Matrix Proteins in Mollusks.Molecular biology and evolution · 2022Article
- Domain Expansion and Functional Diversification in Vertebrate Reproductive Proteins.Molecular biology and evolution · 2022Article
- The kidney releases a nonpolymerizing form of uromodulin in the urine and circulation that retains the external hydrophobic patch domain.American journal of physiology. Renal physiology · 2022Article
- Mouse zona pellucida proteins as receptors for binding of sperm to eggs.Trends in developmental biology · 2022Article
- Zona Pellucida Genes and Proteins: Essential Players in Mammalian Oogenesis and Fertility.Genes · 2021Review
- Proteomics support the threespine stickleback egg coat as a protective oocyte envelope.Molecular reproduction and development · 2021Article
- Article
- Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.The EMBO journal · 2020Article
- A C. elegans Zona Pellucida domain protein functions via its ZPc domain.PLoS genetics · 2020Article
- Molecular Evolutionary Analysis of Nematode Zona Pellucida (ZP) Modules Reveals Disulfide-Bond Reshuffling and Standalone ZP-C Domains.Genome biology and evolution · 2020Article
- Zona pellucida genes and proteins and human fertility.Trends in developmental biology · 2020Article
- PLAC1: biology and potential application in cancer immunotherapy.Cancer immunology, immunotherapy : CII · 2019Review
- Morphogenesis of neurons and glia within an epithelium.Development (Cambridge, England) · 2019Article
Corrections and comments
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4 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundHundreds of extracellular proteins polymerise into filaments and matrices by using zona pellucida (ZP) domains. ZP domain proteins perform highly diverse functions, ranging from structural to receptorial, and mutations in their genes are responsible for a number of severe human diseases. Recently, PLAC1, Oosp1-3, Papillote and CG16798 proteins were identified that share sequence homology with the N-terminal half of the ZP domain (ZP-N), but not with its C-terminal half (ZP-C). The functional significance of this partial conservation is unknown.
resultsBy exploiting a highly engineered bacterial strain, we expressed in soluble form the PLAC1-homology region of mammalian sperm receptor ZP3 as a fusion to maltose binding protein. Mass spectrometry showed that the 4 conserved Cys residues within the ZP-N moiety of the fusion protein adopt the same disulfide bond connectivity as in full-length native ZP3, indicating that it is correctly folded, and electron microscopy and biochemical analyses revealed that it assembles into filaments.
conclusionThese findings provide a function for PLAC1-like proteins and, by showing that ZP-N is a biologically active folding unit, prompt a re-evaluation of the architecture of the ZP domain and its polymers. Furthermore, they suggest that ZP-C might play a regulatory role in the assembly of ZP domain protein complexes.
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