ArticleThe Journal of biological chemistry2012
Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 51 citations in OpenAlex.
- On the mechanism of ezrin activation.Biophysical journal · 2026Article
- The unphosphorylated, closed form of ezrin binds to RNA to maintain a metastatic phenotype in osteosarcoma cells.Science signaling · 2026Article
- On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025Article
- An ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode.Biophysical journal · 2023Article
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins.Biophysical reviews · 2022Review
- MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells.Cell reports · 2021Article
- Developmental clock and mechanism of de novo polarization of the mouse embryo.Science (New York, N.Y.) · 2020Article
- Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020Review
- Tools of the trade: studying actin in zebrafish.Histochemistry and cell biology · 2020Review
- Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dorsal convergence of gastrula cells requires Vangl2 and an adhesion protein-dependent change in protrusive activity.Development (Cambridge, England) · 2019Article
- Dynamic structure of the full-length scaffolding protein NHERF1 influences signaling complex assembly.The Journal of biological chemistry · 2019Article
- Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition.International journal of molecular sciences · 2019Review
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- Article
- α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin.Biophysical journal · 2018Article
- Molecular Dynamics of the Association of L-Selectin and FERM Regulated by PIP2.Biophysical journal · 2018Article
- Role of Phosphorylation in Moesin Interactions with PIPBiophysical journal · 2018Article
- Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics.Journal of molecular biology · 2017Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Ezrin is a member of the ezrin-radixin-moesin family (ERM) of adapter proteins that are localized at the interface between the cell membrane and the cortical actin cytoskeleton, and they regulate a variety of cellular functions. The structure representing a dormant and closed conformation of an ERM protein has previously been determined by x-ray crystallography. Here, using contrast variation small angle neutron scattering, we reveal the structural changes of the full-length ezrin upon binding to the signaling lipid phosphatidylinositol 4,5-bisphosphate (PIP(2)) and to F-actin. Ezrin binding to F-actin requires the simultaneous binding of ezrin to PIP(2). Once bound to F-actin, the opened ezrin forms more extensive contacts with F-actin than generally depicted, suggesting a possible role of ezrin in regulating the interfacial structure and dynamics between the cell membrane and the underlying actin cytoskeleton. In addition, using gel filtration, we find that the conformational opening of ezrin in response to PIP(2) binding is cooperative, but the cooperativity is disrupted by a phospho-mimic mutation S249D in the 4.1-ezrin/radixin/moesin (FERM) domain of ezrin. Using surface plasmon resonance, we show that the S249D mutation weakens the binding affinity and changes the kinetics of 4.1-ERM to PIP(2) binding. The study provides the first structural view of the activated ezrin bound to PIP(2) and to F-actin.
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Registered trials
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