ArticleThe Journal of biological chemistry2015
Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
- Radixin: Roles in the Nervous System and Beyond.Biomedicines · 2024Review
- Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular basis of PIP2-dependent conformational switching of phosphorylated CD44 in binding FERM.Biophysical journal · 2023Article
- An ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode.Biophysical journal · 2023Article
- Molecular mechanism of CD44 homodimerization modulated by palmitoylation and membrane environments.Biophysical journal · 2022Article
- Cotranslational interaction of human EBP50 and ezrin overcomes masked binding site during complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 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
- Roles of Virion-Incorporated CD162 (PSGL-1), CD43, and CD44 in HIV-1 Infection of T Cells.Viruses · 2021Review
- A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes.Molecules (Basel, Switzerland) · 2021Article
- Article
- Bidirectional Tumor-Promoting Activities of Macrophage Ezrin.International journal of molecular sciences · 2020Article
- Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.International journal of molecular sciences · 2020Review
- Review
- Molecular mechanism for bidirectional regulation of CD44 for lipid raft affiliation by palmitoylations and PIP2.PLoS computational biology · 2020Article
- ERM Proteins at the Crossroad of Leukocyte Polarization, Migration and Intercellular Adhesion.International journal of molecular sciences · 2020Review
- Regulation of actin assembly by PI(4,5)P2 and other inositol phospholipids: An update on possible mechanisms.Biochemical and biophysical research communications · 2018Review
- Decrease in plasma membrane tension triggers PtdIns(4,5)PNature cell biology · 2018Article
- 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
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
The cell adhesion molecule CD44 regulates diverse cellular functions, including cell-cell and cell-matrix interaction, cell motility, migration, differentiation, and growth. In cells, CD44 co-localizes with the membrane-cytoskeleton adapter protein Ezrin that links the CD44 assembled receptor signaling complexes to the cytoskeletal actin network, which organizes the spatial and temporal localization of signaling events. Here we report that the cytoplasmic tail of CD44 (CD44ct) is largely disordered. Upon binding to the signaling lipid phosphatidylinositol 4,5-bisphosphate (PIP2), CD44ct clusters into aggregates. Further, contrary to the generally accepted model, CD44ct does not bind directly to the FERM domain of Ezrin or to the full-length Ezrin but only forms a complex with FERM or with the full-length Ezrin in the presence of PIP2. Using contrast variation small angle neutron scattering, we show that PIP2 mediates the assembly of a specific heterotetramer complex of CD44ct with Ezrin. This study reveals the role of PIP2 in clustering CD44 and in assembling multimeric CD44-Ezrin complexes. We hypothesize that polyvalent electrostatic interactions are responsible for the assembly of CD44 clusters and the multimeric PIP2-CD44-Ezrin complexes.
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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.