ArticleThe Journal of biological chemistry2014
Phosphatidylinositol 4,5-bisphosphate alters the number of attachment sites between ezrin and actin filaments: a colloidal probe study.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 48 citations in OpenAlex.
- The LOK C-terminus is an IBAR-like domain that facilitates membrane binding and ezrin colocalization.Biophysical journal · 2026Article
- Extra-ciliary role for polycystins in regulation of Ezrin and renal tubular morphology.bioRxiv : the preprint server for biology · 2025Article
- Pip5k1γ regulates axon formation by limiting Rap1 activity.Life science alliance · 2024Article
- Actomyosin Activity and Piezo1 Activity Synergistically Drive Urinary System Fibroblast Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Three membrane fusion pore families determine the pathway to pore dilation.Biophysical journal · 2023Article
- Review
- Bioinspired Membrane Interfaces: Controlling Actomyosin Architecture and Contractility.ACS applied materials & interfaces · 2023Article
- Reversal of ciliary mechanisms of disassembly rescues olfactory dysfunction in ciliopathies.JCI insight · 2022Article
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- The ROCK-ezrin signaling pathway mediates LPS-induced cytokine production in pulmonary alveolar epithelial cells.Cell communication and signaling : CCS · 2022Article
- A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins.Biophysical reviews · 2022Review
- Role of Ezrin in Asthma-Related Airway Inflammation and Remodeling.Mediators of inflammation · 2022Review
- Membrane fusion studied by colloidal probes.European biophysics journal : EBJ · 2021Review
- Actin-Membrane Release Initiates Cell Protrusions.Developmental cell · 2020Article
- C-terminal phosphorylation modulates ERM-1 localization and dynamics to control cortical actin organization and support lumen formation duringDevelopment (Cambridge, England) · 2020Article
- Molecular mechanism for bidirectional regulation of CD44 for lipid raft affiliation by palmitoylations and PIP2.PLoS computational biology · 2020Article
- 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
- Ezrin Phosphorylation at T567 Modulates Cell Migration, Mechanical Properties, and Cytoskeletal Organization.International journal of molecular sciences · 2020Article
- Article
- Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Direct linkage between the plasma membrane and the actin cytoskeleton is controlled by the protein ezrin, a member of the ezrin-radixin-moesin protein family. To function as a membrane-cytoskeleton linker, ezrin needs to be activated in a process that involves binding of ezrin to phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphorylation of a conserved threonine residue. Here, we used colloidal probe microscopy to quantitatively analyze the interaction between ezrin and F-actin as a function of these activating factors. We show that the measured individual unbinding forces between ezrin and F-actin are independent of the activating parameters, in the range of approximately 50 piconewtons. However, the cumulative adhesion energy greatly increases in the presence of PIP2 demonstrating that a larger number of bonds between ezrin and F-actin has formed. In contrast, the phosphorylation state, represented by phosphor-mimetic mutants of ezrin, only plays a minor role in the activation process. These results are in line with in vivo experiments demonstrating that an increase in PIP2 concentration recruits more ezrin to the apical plasma membrane of polarized cells and significantly increases the membrane tension serving as a measure of the adhesion sites between the plasma membrane and the F-actin network.
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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.