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The cytoplasmic peripheral membrane protein encoded by EZR functions as a protein-tyrosine kinase substrate in microvilli. Additionally we are shipping Ezrin Antibodies (318) and Ezrin Kits (43) and many more products for this protein.
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Suggest a role for ezrin in advanced glycation end product-induced podocyte damage.
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.
Activation of liver PKCs during cholestasis leads to Ezrin Thr567 phosphorylation resulting in MRP2 (show ABCC2 Proteins) internalization and degradation where ubiquitin ligase E3 GP78 (show AMFR Proteins) is involved.
Data indicate that a quinoline-based small molecule, NSC305787, directly binds to ezrin and inhibits its functions.
We identified and confirmed that Fra-1 (show FOSL1 Proteins) affected the expression level of CTTN (show CTTN Proteins) and EZR in vitro through LC-MS/MS analyses and western blot technology.
Data show that both Ezrin and SIX1 (show SIX1 Proteins) proteins are highly expressed in alpha fetoprotein (show AFP Proteins)-negative hepatocellular carcinoma (HCC (show FAM126A Proteins)) and significantly related with the TNM (show ODZ1 Proteins) stage.
it was found that expression of miR (show MLXIP Proteins)-96 was negatively correlated with the metastatic ability of renal cell carcinoma (show MOK Proteins), and that downregulation of miR (show MLXIP Proteins)-96 could suppress the invasion of renal cancer cell via downregulation of Ezrin expression.
These findings are important in understanding the interrelation and dynamics of a CHP1 (show CHP Proteins)-ezrin-NHE3 (show SLC9A3 Proteins) regulatory complex.
ezrin controls the translation of mRNAs preferentially with a structured 5' untranslated region, at least in part, by sustaining the protein level of DDX3 (show DDX3X Proteins) and/or regulating its function.
EZR, CLIC5 (show CLIC5 Proteins) and PODXL (show PODXL Proteins) are overexpressed in hepatocellular carcinoma and may have a role in cell migration and invasiveness
Ezrin and CK18 (show KRT18 Proteins) are downregulated during implantation in cattle. The expression changes represent a temporal depolarization, which could be important for an establishment of bovine pregnancy.
Ezrin-dependent, membrane-specific translocation and activation of calpain by VEGF (show VEGFA Proteins) precedes AMPK (show PRKAA1 Proteins) and AKT (show AKT1 Proteins)-dependent phosphorylation of eNOSs1179 and production of NO.
Data, including data from studies in knockout mice, suggest that VDR (vitamin D receptor) regulates expression of ezrin in enterocytes; VDR (show CYP27B1 Proteins) appears not to be involved in morphology of tight junctions and absorption of large molecules in enterocytes.
Lack of ezrin not only causes achlorhydria and hypergastrinemia but also changes the structure of gastric glands, with severe perturbation of the secretory membranes of parietal cells.
our study demonstrates that ezrin is a novel regulator of IL-10 (show IL10 Proteins) production by B cells
Merlin (show NF2 Proteins) and Ezrin are components of a mechanism where mechanical forces associated with cell junctions are transduced across the cell cortex via cortical actomyosin cytoskeleton to control lateral mobility and activity of epidermal growth factor receptor (show EGFR Proteins).
Dysfunction of ezrin mimics important aspects of the pathological mechanisms responsible for cholangiopathies
We hypothesize that polyvalent electrostatic interactions are responsible for the assembly of CD44 (show CD44 Proteins) clusters and the multimeric PIP2-CD44 (show CD44 Proteins)-Ezrin complexes.
These results indicate that ezrin is required for uptake of hypotaurine from maternal serum by placental trophoblasts, and plays an important role in fetal growth.
These data altogether suggest a novel role of ezrin in the neuritogenesis of the cultured cortical neurons through down-regulation of RhoA (show RHOA Proteins) activity.
Beta-dystroglycan can respond to ezrin driven cytoskeletal and cell morphology changes,by translocating from the cytoplasm to the nucleus.
The findings demonstrate that adult neural stem cells and neuroblasts express ezrin and that ezrin may be involved in intracellular actin remodeling.
The cytoskeletal linker protein (show LAT Proteins) ezrin plays a significant role in hypothermic preservation injury in renal epithelia.
Coexpression of ezrin with Eps8 promotes the formation of membrane ruffles and tufts of microvilli, whereas expression of ezrin and Eps8L1a induces the clustering of actin-containing structures at the cell surface.
These findings reveal that direct ezrin interactions promote PTH1R apical localization and signaling in LLC-PK1 cells.
Spatial control of proton pump H,K-ATPase (show ATP1A1 Proteins) docking at the apical membrane by phosphorylation-coupled ezrin-syntaxin 3 (show STX3 Proteins) interaction.
1) NHE3 (show SLC9A3 Proteins) basal activity is regulated by a signaling complex that is controlled by sequential effects of two kinases, Akt (show AKT1 Proteins) and GSK-3, which act on a Ser (show SIGLEC1 Proteins) cluster in the same NHE3 (show SLC9A3 Proteins) C-terminal domain that binds ezrin
Ezrin-mediated F-actin interaction with the epithelial cell may direct membrane recruitment and cytoskeletal surface extension.
relatively high turnover of ezrin T567 phosphorylation was observed in all three epithelia (gastric, kidney and intestine).
VLN2 and VLN3 act redundantly in sclerenchyma development via bundling of actin filaments.
Data indicate that the construction of actin collars was affected in vln2 vln5 double mutantpollen tubes.
VLN2 and VLN3 play a role in actin filament organization in Arabidopsis.
The cytoplasmic peripheral membrane protein encoded by this gene functions as a protein-tyrosine kinase substrate in microvilli. As a member of the ERM protein family, this protein serves as an intermediate between the plasma membrane and the actin cytoskeleton. This protein plays a key role in cell surface structure adhesion, migration and organization, and it has been implicated in various human cancers. A pseudogene located on chromosome 3 has been identified for this gene. Alternatively spliced variants have also been described for this gene.
, villin 2 (ezrin)
, cytovillin 2