ArticleJournal of dental research2020
An Evolutionarily Conserved Helix Mediates Ameloblastin-Cell Interaction.
Article in Journal of dental research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 12 citations in OpenAlex.
- Ameloblastin amphipathic helix motif mediates ameloblast polarization and prismatic enamel formation.International journal of oral science · 2026Article
- Ameloblastin Amphipathic Helix Motif mediates Ameloblast Polarization and Prismatic Enamel Formation via a RhoA Signaling Pathway.Research square · 2026Article
- Ameloblastin binding to biomimetic models of cell membranes - A continuum of intrinsic disorder.Archives of oral biology · 2025Article
- Deletion within ameloblastin multitargeting domain reduces its interaction with artificial cell membrane.Journal of structural biology · 2024Article
- Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
- Physicochemical understanding of biomineralization by molecular vibrational spectroscopy: From mechanism to nature.Exploration (Beijing, China) · 2023Review
- The Dynamic Interactions of a Multitargeting Domain in Ameloblastin Protein with Amelogenin and Membrane.International journal of molecular sciences · 2023Article
- Revisiting ameloblastin; addressing the EMT-ECM axis above and beyond oral biology.Frontiers in cell and developmental biology · 2023Article
- Coemergence of the Amphipathic Helix on Ameloblastin With Mammalian Prismatic Enamel.Molecular biology and evolution · 2022Article
- Modeling ameloblast-matrix interactions using 3D cell culture.Frontiers in physiology · 2022Article
- Ameloblastin promotes polarization of ameloblast cell lines in a 3-D cell culture system.Matrix biology : journal of the International Society for Matrix Biology · 2022Article
- Co-Immunoprecipitation Reveals Interactions Between Amelogenin and AmeloblastinFrontiers in physiology · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ameloblastin (Ambn) has the potential to regulate cell-matrix adhesion through familiar cell-binding domains, but the proposed sequence motifs are not highly conserved across species. Here, we report that Ambn binds to ameloblast-like cell membranes through a highly evolutionary conserved amphipathic helix-forming (AH) motif encoded by exon 5. We applied high-resolution confocal microscopy to show colocalization of Ambn with ameloblast membrane surfaces in developing mouse incisors. Using a series of Ambn-derived peptides and Ambn variants, we showed that Ambn binds to cell membranes through a motif within the sequence encoded by exon 5. Using peptides derived from the N- or C-termini of this sequence, as well as Ambn variants that lacked or had a disrupted AH motif, we demonstrated that the AH motif located at the N-terminus of the sequence is involved in cell-Ambn adhesion. Sequence analysis revealed that this highly conserved AH motif is absent from other enamel matrix proteins, including amelogenin, enamelin, and amelotin. Collectively, these data suggest that Ambn binds to the cell surface membrane via a helix-forming motif and provide insight into the molecular mechanism and function of Ambn in enamel cell-matrix interaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.