Disease relevance of Rdx

• The expression of the two cytoskeletal linking proteins, moesin and radixin, was examined in experimental mesangial proliferative nephritis in rats (anti-Thy1 model) [1].
• The cytoskeletal linking proteins, moesin and radixin, are upregulated by platelet-derived growth factor, but not basic fibroblast growth factor in experimental mesangial proliferative glomerulonephritis [1].
• This concentration of radixin at the cleavage furrow was detected in all other cultured cells we examined: bovine epithelial cells (MDBK cells), mouse myeloma cells (P3 cells), rat kangaroo Ptk2 cells, mouse teratocarcinoma cells, and chicken fibroblasts [2].

High impact information on Rdx

• The increase in these cytoskeletal proteins appears to be regulated primarily (radixin) or partially (moesin) posttranscriptionally [1].
• Moesin and radixin mRNA and protein are constitutively expressed in all cell types of normal rat glomeruli, except podocytes [1].
• The data suggest that PDGF mediated upregulation of the cytoskeletal proteins, moesin and radixin, is important for cell migration and other changes that accompany the coordinated restoration of glomerular architecture after injury [1].
• Suppression of radixin and moesin alters growth cone morphology, motility, and process formation in primary cultured neurons [3].
• Taken collectively, our data suggest that by regulating key aspects of growth cone development and maintenance, radixin and moesin modulate neurite formation and the development of neuronal polarity [3].

Biological context of Rdx

• Furthermore, the expression level of membranous RhoA and phosphorylation of the target proteins of Rho-kinase, the ERM (ezrin, radixin, moesin) family members, was significantly greater in L-NAME-treated rats than in control rats [4].
• Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis [2].
• Radixin appeared to accumulate rapidly at the cleavage furrow at the onset of furrowing, continued to be concentrated at the furrow during anaphase and telophase, and was finally enriched at the midbody [2].

Anatomical context of Rdx

• In the adult rat RPE, only ezrin (no moesin or radixin) was detected at high levels by immunofluorescence and immunoelectron microscopy at microvilli and basal infoldings [5].
• Cultured Schwann cells express high levels of all three proteins and the ezrin-binding protein 50, whereas neurons express much lower, although detectable, levels of radixin and moesin [6].
• Distinct from its other family members, moesin and radixin, which are predominantly expressed in glomerular endothelial and mesangial areas, ezrin protein (by immunohistochemistry) was specifically and exclusively modulated during podocyte injury and regeneration [7].
• In the anti-Thy1 model the expression of moesin and radixin was increased in infiltrating macrophages and in activated, alpha-smooth muscle actin-positive mesangial cells and was concentrated in the cellular extensions of mesangial cells in areas of glomerular remodelling [1].
• A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization [8].

Other interactions of Rdx

• Specific knockdown of Mrp2 (approximately 50% decrease in expression) resulted in an approximately 45% decrease in the biliary excretion index of carboxydichlorofluorescein (CDF) (9.3% versus 16.5%), but did not affect Mrp3 or radixin expression [9].

References