ArticleThe Journal of cell biology2000
Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 236 citations in OpenAlex.
- On the mechanism of ezrin activation.Biophysical journal · 2026Article
- Structural and Dynamic Insights into Podocalyxin-Ezrin Interaction as a Target in Cancer Progression.Journal of xenobiotics · 2026Article
- On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025Article
- TNIK: A redox sensor in endothelial cell permeability.Science advances · 2024Article
- HIV Infection: Shaping the Complex, Dynamic, and Interconnected Network of the Cytoskeleton.International journal of molecular sciences · 2023Review
- FERM domains recruit ample PI(4,5)PBiophysical journal · 2023Article
- The ERM-1 membrane-binding domain directs erm-1 mRNA localization to the plasma membrane in the C. elegans embryo.Development (Cambridge, England) · 2022Article
- Pathophysiological Roles of Actin-Binding Scaffold Protein, Ezrin.International journal of molecular sciences · 2022Review
- ERM-1 Phosphorylation and NRFL-1 Redundantly Control Lumen Formation in theFrontiers in cell and developmental biology · 2022Article
- Role of Ezrin in Asthma-Related Airway Inflammation and Remodeling.Mediators of inflammation · 2022Review
- C-terminal phosphorylation modulates ERM-1 localization and dynamics to control cortical actin organization and support lumen formation duringDevelopment (Cambridge, England) · 2020Article
- Shigella impairs human T lymphocyte responsiveness by hijacking actin cytoskeleton dynamics and T cell receptor vesicular trafficking.Cellular microbiology · 2020Article
- Light-responsive microRNA miR-211 targets Ezrin to modulate lysosomal biogenesis and retinal cell clearance.The EMBO journal · 2020Article
- Critical roles of phosphoinositides and NF2 in Hippo pathway regulation.Genes & development · 2020Article
- Phosphoinositides: multipurpose cellular lipids with emerging roles in cell death.Cell death and differentiation · 2019Review
- Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition.International journal of molecular sciences · 2019Review
- Neutrophil Cell Shape Change: Mechanism and Signalling during Cell Spreading and Phagocytosis.International journal of molecular sciences · 2019Review
- Serine Phosphorylation of L-Selectin Regulates ERM Binding, Clustering, and Monocyte Protrusion in Transendothelial Migration.Frontiers in immunology · 2019Article
- L-selectin: A Major Regulator of Leukocyte Adhesion, Migration and Signaling.Frontiers in immunology · 2019Review
- Merlin/ERM proteins regulate growth factor-induced macropinocytosis and receptor recycling by organizing the plasma membrane:cytoskeleton interface.Genes & development · 2018Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoskeleton-membrane linker protein ezrin has been shown to associate with phosphatidyl-inositol 4,5-bisphosphate (PIP(2))-containing liposomes via its NH(2)-terminal domain. Using internal deletions and COOH-terminal truncations, determinants of PIP(2) binding were located to amino acids 12-115 and 233-310. Both regions contain a KK(X)(n)K/RK motif conserved in the ezrin/radixin/moesin family. K/N mutations of residues 253 and 254 or 262 and 263 did not affect cosedimentation of ezrin 1-333 with PIP(2)-containing liposomes, but their combination almost completely abolished the capacity for interaction. Similarly, double mutation of Lys 63, 64 to Asn only partially reduced lipid interaction, but combined with the double mutation K253N, K254N, the interaction of PIP(2) with ezrin 1-333 was strongly inhibited. Similar data were obtained with full-length ezrin. When residues 253, 254, 262, and 263 were mutated in full-length ezrin, the in vitro interaction with the cytoplasmic tail of CD44 was not impaired but was no longer PIP(2) dependent. This construct was also expressed in COS1 and A431 cells. Unlike wild-type ezrin, it was not any more localized to dorsal actin-rich structures, but redistributed to the cytoplasm without strongly affecting the actin-rich structures. We have thus identified determinants of the PIP(2) binding site in ezrin whose mutagenesis correlates with an altered cellular localization.
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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.