ArticleThe Journal of cell biology1995
Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 108 citations in OpenAlex.
- Measuring and manipulating localized translation of erm-1 in the C. elegans embryo.Development (Cambridge, England) · 2025Article
- The regulation of actin dynamics during cell division and malignancy.American journal of cancer research · 2021Review
- Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2.Nature communications · 2018Article
- The proteome of the differentiating mesencephalic progenitor cell line CSM14.1 in vitro.BioMed research international · 2014Article
- G protein-coupled receptor kinase 2 activates radixin, regulating membrane protrusion and motility in epithelial cells.Biochimica et biophysica acta · 2010Article
- ERM proteins regulate growth cone responses to Sema3A.The Journal of comparative neurology · 2008Article
- Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell.The EMBO journal · 2005Article
- Radixin deficiency causes deafness associated with progressive degeneration of cochlear stereocilia.The Journal of cell biology · 2004Article
- Role for moesin in lipopolysaccharide-stimulated signal transduction.Infection and immunity · 2004Article
- Article
- Characterization of human palladin, a microfilament-associated protein.Molecular biology of the cell · 2001Article
- The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association.The Biochemical journal · 2001Article
- 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.The Journal of cell biology · 2000Article
- Imaging of dynamic changes of the actin cytoskeleton in microextensions of live NIH3T3 cells with a GFP fusion of the F-actin binding domain of moesin.BMC cell biology · 2000Article
- Ezrin promotes morphogenesis of apical microvilli and basal infoldings in retinal pigment epithelium.The Journal of cell biology · 1999Article
- Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins.The Journal of cell biology · 1999Article
- Radixin is involved in lamellipodial stability during nerve growth cone motility.Molecular biology of the cell · 1999Article
- Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons.The Journal of cell biology · 1998Article
- Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles.The Journal of cell biology · 1998Article
- Calpain regulates actin remodeling during cell spreading.The Journal of cell biology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The ERM proteins--ezrin, radixin, and moesin--occur in particular cortical cytoskeletal structures. Several lines of evidence suggest that they interact with both cytoskeletal elements and plasma membrane components. Here we described the properties of full-length and truncated radixin polypeptides expressed in transfected cells. In stable transfectants, exogenous full-length radixin behaves much like endogenous ERM proteins, localizing to the same cortical structures. However, the presence of full-length radixin or its carboxy-terminal domain in cortical structures correlates with greatly diminished staining of endogenous moesin in those structures, suggesting that radixin and moesin compete for a limiting factor required for normal associations in the cell. The results also reveal distinct roles for the amino- and carboxy-terminal domains. At low levels relative to endogenous radixin, the carboxy-terminal polypeptide is associated with most of the correct cortical targets except cleavage furrows. In contrast, the amino-terminal polypeptide is diffusely localized throughout the cell. Low level expression of full-length radixin or either of the truncated polypeptides has no detectable effect on cell physiology. However, high level expression of the carboxy-terminal domain dramatically disrupts normal cytoskeletal structures and functions. At these high levels, the amino-terminal polypeptide does localize to cortical structures, but does not affect the cells. We conclude that the behavior of radixin in cells depends upon activities contributed by separate domains of the protein, but also requires modulating interactions between those domains.
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