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Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. Additionally we are shipping Radixin Antibodies (108) and Radixin Kits (8) and many more products for this protein.
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Phospho-Ezrin/Radixin/Moesin (ERM (show MSN Proteins)) inhibit cell adhesion, and therefore, dephosphorylation of ERM (show ETV5 Proteins) proteins is essential for cell adhesion.Phospho-ERM (show ETV5 Proteins) induce formation and/or maintenance of spherical cell shape.
These studies identify Akt2 (show AKT2 Proteins) as a critical kinase that regulates radixin phosphorylation and leads to Mrp-2 (show ABCC2 Proteins) translocation and function.
Intracellular sphingosine kinase 2 (show SPHK2 Proteins)-derived sphingosine-1-phosphate mediates epidermal growth factor (show EGF Proteins)-induced ezrin-radixin-moesin (show MSN Proteins) phosphorylation and cancer cell invasion.
High Radixin expression is associated with glioblastoma.
Ezrin (show EZR Proteins), radixin and moesin (show MSN Proteins) are unlikely targets for autoantibodies in demyelinating neuropathies.
Data show that silencing ezrin-radixin-moesin (ERM (show MSN Proteins)) protein expression ablates deleted in colorectal carcinoma (show DCC Proteins) protein (DCC (show DCC Proteins))-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 (show ESR1 Proteins)
Radixin was identified as a target gene of miR (show MLXIP Proteins)-196a/-196b. Elevated miR (show MLXIP Proteins)-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 (show Vip Proteins) regulates CFTR (show CFTR Proteins) membrane expression and function in Calu (show CALU Proteins)-3 cells by increasing its interaction with NHERF1 (show SLC9A3R1 Proteins) and P-ERM (show ETV5 Proteins) in a VPAC1 (show VIPR1 Proteins)- and PKCepsilon (show PRKCE Proteins)-dependent manner.
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 (show POSTN Proteins)-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 (show ICAM5 Proteins) play a pivotal role in the phosphorylation of ezrin/radixin/moesin (show MSN Proteins) proteins and the formation of phagocytic cup-like structures on neuronal dendrites
Ezrin/radixin/moesin (show MSN Proteins) are required for the purinergic P2X7 receptor (P2X7R (show P2RX7 Proteins))-dependent processing of the amyloid precursor protein (show APP Proteins).
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 (show MSN Proteins)) proteins are induced in activated microglia/macrophages, whereas ERM (show ETV5 Proteins) molecules are only marginally expressed in quiescent microglia in the normal brain.
Ezrin (show EZR Proteins), radixin, and moesin (show MSN Proteins) are phosphorylated in response to 2-methoxyestradiol and modulate endothelial hyperpermeability.
Results show that while CD43 (show SPN Proteins) binding to ezrin-radixin-moesin (show MSN Proteins) proteins is crucial for S76 phosphorylation, CD43 (show SPN Proteins) movement and regulation of T-cell migration can occur through an ERM (show ETV5 Proteins)-independent, phosphorylation-dependent mechanism.
Radixin inactivation causes hyperbilirubinemia (likely due to a defect in the localization Multidrug resistance protein 2 (show ABCC2 Proteins) in the bile canalicular membranes) and deafness due to progressive degeneration of cochlear stereocilia. (Review)
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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