ArticleThe Journal of cell biology1989
A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 208 citations in OpenAlex.
- Moesin controls cell-cell fusion and osteoclast function.The Journal of cell biology · 2025Article
- Ezrin, radixin, and moesin are dispensable for macrophage migration and cellular cortex mechanics.The EMBO journal · 2024Article
- Comparison of thermal and athermal dynamics of the cell membrane slope fluctuations in the presence and absence of Latrunculin-B.Physical biology · 2023Article
- Pre-organized landscape of T cell surface.Frontiers in immunology · 2023Review
- The ERM-1 membrane-binding domain directs erm-1 mRNA localization to the plasma membrane in the C. elegans embryo.Development (Cambridge, England) · 2022Article
- Moesin Serves as Scaffold Protein for PD-L1 in Human Uterine Cervical Squamous Carcinoma Cells.Journal of clinical medicine · 2022Article
- Prominin-1-Radixin axis controls hepatic gluconeogenesis by regulating PKA activity.EMBO reports · 2020Article
- ERM Proteins at the Crossroad of Leukocyte Polarization, Migration and Intercellular Adhesion.International journal of molecular sciences · 2020Review
- Global long non-coding RNA expression in the rostral anterior cingulate cortex of depressed suicides.Translational psychiatry · 2018Article
- Kindlin-2 directly binds actin and regulates integrin outside-in signaling.The Journal of cell biology · 2016Article
- Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturation.The Journal of cell biology · 2015Article
- The ezrin-radixin-moesin family of proteins in the regulation of B-cell immune response.Critical reviews in immunology · 2015Review
- Activation of ezrin/radixin/moesin mediates attractive growth cone guidance through regulation of growth cone actin and adhesion receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Expression of the ERM family members (ezrin, radixin and moesin) in breast cancer.Experimental and therapeutic medicine · 2010Article
- Discovering the molecular components of intercellular junctions--a historical view.Cold Spring Harbor perspectives in biology · 2009Review
- Expression, localization, and binding activity of the ezrin/radixin/moesin proteins in the mouse testis.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2009Article
- ERM proteins regulate growth cone responses to Sema3A.The Journal of comparative neurology · 2008Article
- Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin.The Journal of cell biology · 2007Article
- The expression of ezrin in NPC and its interaction with NGX6, a novel candidate suppressor.Cancer science · 2007Article
- The nuclear receptor hepatocyte nuclear factor 4alpha acts as a morphogen to induce the formation of microvilli.The Journal of cell biology · 2006Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An 82-kD protein has been purified from the undercoat of the adherens junction isolated from the rat liver. The purification scheme includes low salt extraction followed by DEAE-cellulose ion exchange, DNase I-actin affinity, and carboxyl methyl-cellulose ion exchange chromatographies. The purified 82-kD protein was essentially free of contaminants as judged by SDS-PAGE combined with silver staining. The substoichiometric 82-kD protein largely inhibited the actin filament assembly; when the molar ratio of the 82-kD protein to G-actin was 1:1,000, the viscosity was reduced to 28% of the control value. Direct electron microscopic studies revealed that the 82-kD protein selectively inhibited monomer addition at the barbed ends of actin filaments. By use of the antibody raised against the 82-kD protein, this protein was shown by immunofluorescence microscopy to be localized at the cell-to-cell adherens junction in various types of cells. In contrast, the 82-kD protein was not concentrated at the cell-to-substrate adherens junctions (focal contacts). These findings have led us to conclude that the 82-kD protein is a barbed end-capping protein which is associated with the undercoat of the cell-to-cell adherens junction. Hence, we have tentatively designated the 82-kD protein as radixin (from the Latin word radix meaning root).
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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.