ArticleACS omega2019
Ameloblastin Binds to Phospholipid Bilayers via a Helix-Forming Motif within the Sequence Encoded by Exon 5.
Article in ACS omega, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Ameloblastin amphipathic helix motif mediates ameloblast polarization and prismatic enamel formation.International journal of oral science · 2026Article
- Circulating extracellular vesicles in plasma carry accessible molecular signatures of aging in mice.bioRxiv : the preprint server for biology · 2026Article
- Ameloblastin Amphipathic Helix Motif mediates Ameloblast Polarization and Prismatic Enamel Formation via a RhoA Signaling Pathway.Research square · 2026Article
- Oligomerization Function of the Native Exon 5 Sequence of Ameloblastin Fused with Calmodulin.ACS omega · 2025Article
- 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
- Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin-Amelogenin Interactions.ACS biomaterials science & engineering · 2023Article
- The Dynamic Interactions of a Multitargeting Domain in Ameloblastin Protein with Amelogenin and Membrane.International journal of molecular sciences · 2023Article
- Overexpression of ameloblastin in secretory ameloblasts results in demarcated, hypomineralized opacities in enamel.Frontiers in physiology · 2023Article
- Coemergence of the Amphipathic Helix on Ameloblastin With Mammalian Prismatic Enamel.Molecular biology and evolution · 2022Article
- Highly acidic pH facilitates enamel protein self-assembly, apatite crystal growth and enamel protein interactions in the early enamel matrix.Frontiers in physiology · 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
- Characterization of AMBN I and II Isoforms and Study of Their CaInternational journal of molecular sciences · 2020Article
- An Evolutionarily Conserved Helix Mediates Ameloblastin-Cell Interaction.Journal of dental research · 2020Article
- A missense variant in specificity protein 6 (SP6) is associated with amelogenesis imperfecta.Human molecular genetics · 2020Article
- Co-Immunoprecipitation Reveals Interactions Between Amelogenin and AmeloblastinFrontiers in physiology · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Ameloblastin (Ambn), the most abundant non-amelogenin enamel protein, is intrinsically disordered and has the potential to interact with other enamel proteins and with cell membranes. Here, through multiple biophysical methods, we investigated the interactions between Ambn and large unilamellar vesicles (LUVs), whose lipid compositions mimicked cell membranes involved in epithelial cell-extracellular matrix adhesion. Using a series of Ambn Trp/Phe variants and Ambn mutants, we further showed that Ambn binds to LUVs through a highly conserved motif within the sequence encoded by exon 5. Synthetic peptides derived from different regions of Ambn confirmed that the sequence encoded by exon 5 is involved in LUV binding. Sequence analysis of Ambn across different species showed that the N-terminus of this sequence contains a highly conserved motif with a propensity to form an amphipathic helix. Mutations in the helix-forming sequence resulted in a loss of peptide binding to LUVs. Our in vitro data suggest that Ambn binds the lipid membrane directly through a conserved helical motif and have implications for biological events such as Ambn-cell interactions, Ambn signaling, and Ambn secretion via secretory vesicles.
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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.