ArticleJournal of molecular biology2019
Intestinal Gel-Forming Mucins Polymerize by Disulfide-Mediated Dimerization of D3 Domains.
Article in Journal of molecular biology, 2019. 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, 49 citations in OpenAlex.
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- Astroviruses use mucus secretion as a novel form of viral egress.PLoS pathogens · 2026Article
- Dynamic glycan network engineering of native mucin enables reversible, self-healing, and adhesive hydrogel interfaces.Nanoscale advances · 2026Article
- EatA mediated degradation of intestinal mucus is species-specific and driven by MUC2 structural features.Nature communications · 2025Article
- Cryo-EM structure of native honey bee vitellogenin.Nature communications · 2025Article
- Mucins and Their Roles in Asthma.Immunological reviews · 2025Review
- MUC5AC filaments illuminate the structural diversification of respiratory and intestinal mucins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure of the MUC5AC VWD3 assembly responsible for the formation of net-like mucin polymers.EMBO reports · 2025Article
- Emerging cell and molecular targets for treating mucus hypersecretion in asthma.Allergology international : official journal of the Japanese Society of Allergology · 2024Review
- ThePolymers · 2024Review
- The IRE1β-mediated unfolded protein response is repressed by the chaperone AGR2 in mucin producing cells.The EMBO journal · 2024Article
- VWD domain stabilization by autocatalytic Asp-Pro cleavage.Protein science : a publication of the Protein Society · 2024Article
- Hydrogen sulfide responsive nanoplatforms: Novel gas responsive drug delivery carriers for biomedical applications.Asian journal of pharmaceutical sciences · 2024Review
- An Increase in Mucin2 Expression Is Required for Colon Cancer Progression Mediated by L1.International journal of molecular sciences · 2023Article
- Delayed gut microbiota maturation in the first year of life is a hallmark of pediatric allergic disease.Nature communications · 2023Article
- The Regulated Secretion and Models of Intracellular Transport: The Goblet Cell as an Example.International journal of molecular sciences · 2023Review
- The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins.Nature communications · 2023Article
- The disulfide catalyst QSOX1 maintains the colon mucosal barrier by regulating Golgi glycosyltransferases.The EMBO journal · 2023Article
- The role of goblet cells and mucus in intestinal homeostasis.Nature reviews. Gastroenterology & hepatology · 2022Review
- Helical self-assembly of a mucin segment suggests an evolutionary origin for von Willebrand factor tubules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mucin 2 glycoprotein assembles into a complex hydrogel that protects intestinal epithelia and houses the gut microbiome. A major step in mucin 2 assembly is further multimerization of preformed mucin dimers, thought to produce a honeycomb-like arrangement upon hydrogel expansion. Important open questions are how multiple mucin 2 dimers become covalently linked to one another and how mucin 2 multimerization compares with analogous processes in related polymers such as respiratory tract mucins and the hemostasis protein von Willebrand factor. Here we report the x-ray crystal structure of the mucin 2 multimerization module, found to form a dimer linked by two intersubunit disulfide bonds. The dimer structure calls into question the current model for intestinal mucin assembly, which proposes disulfide-mediated trimerization of the same module. Key residues making interactions across the dimer interface are highly conserved in intestinal mucin orthologs, supporting the physiological relevance of the observed quaternary structure. With knowledge of the interface residues, it can be demonstrated that many of these amino acids are also present in other mucins and in von Willebrand factor, further indicating that the stable dimer arrangement reported herein is likely to be shared across this functionally broad protein family. The mucin 2 module structure thus reveals the manner by which both mucins and von Willebrand factor polymerize, drawing deep structural parallels between macromolecular assemblies critical to mucosal epithelia and the vasculature.
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