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Human Radixin Protein expressed in HEK-293 Cells - ABIN2730421
Miyaji, Shahrizaila, Umapathi, Chan, Hirata, Yuki: Are ERM (ezrin/radixin/moesin) proteins targets for autoantibodies in demyelinating neuropathies? in Human immunology 2015
CPI-17 drives Ras activity and tumorigenesis in melanomas in a two-fold way; inactivation of the tumor suppressor merlin and activation of the growth promoting ERM family.
The results reveal a supportive role of ERMs in cortical activities during cytokinesis, and also provide insight into the selective mechanism that preferentially associates cytokinesis-relevant proteins with the division site.
Radixin knockdown suppresses the metastasis of SGC-7901 cells in vitro by up-regulation of E-cadherin. The NF-kappaB/snail pathway contributes to the regulation of E-cadherin in response to depletion of radixin.
Phospho-Ezrin/Radixin/Moesin (ERM) inhibit cell adhesion, and therefore, dephosphorylation of ERM proteins is essential for cell adhesion.Phospho-ERM induce formation and/or maintenance of spherical cell shape.
These studies identify Akt2 as a critical kinase that regulates radixin phosphorylation and leads to Mrp-2 translocation and function.
Intracellular sphingosine kinase 2-derived sphingosine-1-phosphate mediates epidermal growth factor-induced ezrin-radixin-moesin phosphorylation and cancer cell invasion.
High Radixin expression is associated with glioblastoma.
Ezrin, radixin and moesin are unlikely targets for autoantibodies in demyelinating neuropathies.
Data show that silencing ezrin-radixin-moesin (ERM) protein expression ablates deleted in colorectal carcinoma protein (DCC)-protein kinase A (PKA) interaction and specifically blocks netrin-induced PKA activity and phosphorylation.
These data suggest an association between RDX polymorphisms and the clinical features of RA patients, particularly the ESR
Radixin was identified as a target gene of miR-196a/-196b. Elevated miR-196a/-196b expression in GC cells led to reduced radixin protein levels and vice versa.
This study finding have implications concerning the importance of concomitant radixin upregulation in tumor progression and poor prognosis of patients with gliomas.
VIP regulates CFTR membrane expression and function in Calu-3 cells by increasing its interaction with NHERF1 and P-ERM in a VPAC1- and PKCepsilon-dependent manner.
important role of ezrin-moesin-radixin proteins during HCV infection at the postentry level and highlight possible novel targets for HCV treatment.
ERM proteins play important differential roles in the thrombin-induced modulation of EC permeability, with moesin promoting barrier dysfunction and radixin opposing it.
Data suggest that P-glycoprotein associate with the F-actin cytoskeleton through ezrin/radixin/moesin (ERM) in CCR9/CCL25 induced multidrug resistance of acute T-lymphocytic leukemia (T-ALL) cells.
Control of adipogenesis by ezrin, radixin and moesin-dependent biomechanics remodeling.
radixin plays an important role in promoting cell migration by regulating Rac1-mediated epithelial polarity and formation of adherens junctions through Vav GEFs.
Data show that silencing of radixin (RDX) phenocopied the effects of miR-409 overexpression, whereas restoration of RDX in miR-409-overexpressed gastric cancer (GC) cells reversed the suppressive effects of miR-409.
Ezrin/radixin/moesin are required for the purinergic P2X7 receptor (P2X7R)-dependent processing of the amyloid precursor protein.
LRBA deficiency is associated with a reduced abundance of radixin and Nherf2, two adaptor proteins, which are important for the mechanical stability of the basal taper region of stereocilia.
Inactivation of SHIP2 leads to increased microvilli formation and solute reabsorption by the renal proximal tubule and was associated with hyperactivated ezrin/radixin/moesin proteins and increased Rho-GTP.
identification of radixin as a PRG-2 interaction partner and showing that radixin accumulation in growth cones and its LPA-dependent phosphorylation depend on its binding to specific regions within the C-terminal region of PRG-2
This study describes a novel mechanism that regulates plasma receptor pools in the control of synaptic receptor density.
These results indicate that radixin plays an important role in regulating P-glycoprotein localization and P-glycoprotein functional activity at the intestinal membrane.
The specific location of radixin-positive cells in the peri-infarct region and in microglia suggests a role for radixin in microglial activation after stroke.
A Pak1-PP2A-ERM signaling axis mediates F-actin rearrangement and degranulation in mast cells.
the extracellular matrix molecule VN and its neuronal receptor TLCN play a pivotal role in the phosphorylation of ezrin/radixin/moesin proteins and the formation of phagocytic cup-like structures on neuronal dendrites
The ERM (ezrin, radixin, moesin) proteins are novel scaffolds at the level of SOS activity control, which is relevant for both normal Ras function and dysfunction known to occur in several human cancers.
Ezrin-radixin-moesin (ERM) proteins are induced in activated microglia/macrophages, whereas ERM molecules are only marginally expressed in quiescent microglia in the normal brain.
Ezrin, radixin, and moesin are phosphorylated in response to 2-methoxyestradiol and modulate endothelial hyperpermeability.
Results show that while CD43 binding to ezrin-radixin-moesin proteins is crucial for S76 phosphorylation, CD43 movement and regulation of T-cell migration can occur through an ERM-independent, phosphorylation-dependent mechanism.
Radixin inactivation causes hyperbilirubinemia (likely due to a defect in the localization Multidrug resistance protein 2 in the bile canalicular membranes) and deafness due to progressive degeneration of cochlear stereocilia. (Review)
Data suggest that myosin-II and ERM proteins modulate mechanical properties in oocytes, contributing to cell polarity and to completion of meiosis.
The expression pattern demonstrated here suggests a role for radixin in neuronal migration and differentiation in the adult RMS.
Rdx is the dominant ERM protein in the liver of wildtype mice and is concentrated in bile canalicular membranes. Rdx(-/-) mice are normal at birth, but their bilirubin serum concentrations increase at ca. 4 weeks, with mild liver injury at 8 weeks.
Data report the crystal structure of the radixin FERM (4.1 and ERM) domain complexed with the intercellular adhesion molecule-2 (ICAM-2) cytoplasmic peptide.
Key structural and biological properties of the radixin alpha-domain (residues 311-469) are described and its role established in the conformational activation of the ezrin-radixin-moesin family of proteins.
cross talk between the blastocyst and uterus involving the ezrin/radixin/moesin (ERM) proteins and ERM-associated cytoskeletal cross-linker proteins CD43, CD44, ICAM-1, and ICAM-2
Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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