ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-beta binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- A Study on the Clinical Phenotypes and Genetic Analysis ofHuman mutation · 2026Article
- Microvilli control the morphogenesis of the tectorial membrane extracellular matrix.Developmental cell · 2025Article
- Structures of TGF-β with betaglycan and signaling receptors reveal mechanisms of complex assembly and signaling.Nature communications · 2025Article
- Microvilli regulate the release modes of alpha-tectorin to organize the domain-specific matrix architecture of the tectorial membrane.bioRxiv : the preprint server for biology · 2024Article
- Synthesis ofOrganic & biomolecular chemistry · 2023Article
- Computational modeling of TGF-β2:TβRI:TβRII receptor complex assembly as mediated by the TGF-β coreceptor betaglycan.Biophysical journal · 2023Article
- Domain Expansion and Functional Diversification in Vertebrate Reproductive Proteins.Molecular biology and evolution · 2022Article
- The Importance of Gene Duplication and Domain Repeat Expansion for the Function and Evolution of Fertilization Proteins.Frontiers in cell and developmental biology · 2022Review
- Canonical TGFβ Signaling and Its Contribution to Endometrial Cancer Development and Progression-Underestimated Target of Anticancer Strategies.Journal of clinical medicine · 2021Review
- Zona Pellucida Genes and Proteins: Essential Players in Mammalian Oogenesis and Fertility.Genes · 2021Review
- 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
- Structural biology of betaglycan and endoglin, membrane-bound co-receptors of the TGF-beta family.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Lessons from bioengineering the ovarian follicle: a personal perspective.Reproduction (Cambridge, England) · 2019Review
- The release of surface-anchored α-tectorin, an apical extracellular matrix protein, mediates tectorial membrane organization.Science advances · 2019Article
- Galactomannan Pentasaccharide Produced from Copra Meal Enhances Tight Junction Integration of Epithelial Tissue through Activation of AMPK.Biomedicines · 2019Article
- Structural Adaptation in Its Orphan Domain Engenders Betaglycan with an Alternate Mode of Growth Factor Binding Relative to Endoglin.Structure (London, England : 1993) · 2019Article
- TGF-β2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-β and inhibin-α.The Journal of biological chemistry · 2019Article
- Epithelial Shaping by Diverse Apical Extracellular Matrices Requires the Nidogen Domain Protein DEX-1 inGenetics · 2019Article
- Dually modified transmembrane proteoglycans in development and disease.Cytokine & growth factor reviews · 2018Review
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5 authors.
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Abstract
The zona pellucida (ZP) domain is a bipartite protein structural element comprised of ZP-N and ZP-C regions. Most notable for its ability to mediate protein polymerization, many ZP proteins polymerize and assemble into long fibrils that form specialized extracellular matrices. Other ZP proteins (namely, betaglycan and endoglin) do not polymerize but serve as important membrane coreceptors for ligands in the transforming growth factor-β (TGF-β) superfamily. Here, we present the 2.0-Å resolution crystal structure of the betaglycan ZP-C region in combination with a downstream region known as the external hydrophobic patch (EHP). Similar to the ZP-N region, the ZP-C region also adopts an immunoglobulin-like fold, despite sharing no sequence homology and possessing different disulfide linkages. The EHP region, which was previously thought to be external to the ZP region, is integral to the ZP-C domain and corresponds to the ZP-C G strand. Our structure also indicates that the critical maturation cleavage of ZP proteins, a process that activates nascent ZP proteins for polymerization, occurs within the immunoglobulin domain at the FG loop. Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site. Finally, our structure suggests that the AB loop and the convex surface pocket are regions important for TGF-β ligand binding.
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