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Binding of phosphatidylinositol 4,5-biphosphate to ezrin induces a conformational change permitting the insertion of the LOK (Montrer STK10 Kits ELISA) C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK (Montrer STK10 Kits ELISA) kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue.
The expression pattern and subcellular localization of ezrin and moesin (Montrer MSN Kits ELISA) correlate with clinicopathological variables such as patients' age, tumor grade and hormonal status.
Ezrin represents a promising target for the development of strategies aimed at preventing the progression of cervical cancer.
Ezrin S66 phosphorylation enhances filopodia formation, contributing to the regulation of invasion and metastasis of esophageal squamous cell carcinoma cells
Ezrin protein expression is a promising biomarker in estimating the outcome of stage II colorectal cancer patients. When combined with microsatellite status its ability in predicting disease outcome is further improved
Ezrin is down-regulated during cholangiocarcinogenesis, and its loss results in a more aggressive phenotype.
A signature of ezrin-interacting proteins accurately predicts esophageal squamous cell carcinoma patient survival or tumor recurrence.
The results of this meta-analysis suggest that ezrin positive immunoexpression confers a higher risk of recurrence and a worse survival in osteosarcoma patients.
PM blebbing triggered SRF-mediated up-regulation of the metastasis-associated ERM protein Ezrin. Notably, Ezrin is sufficient and important to sustain bleb dynamics for cell-in-cell invasion when SRF is suppressed.
EZR is a novel biomarker in terms of invasion among the 3 subtypes of NFPAs, and it is a promising guide for therapeutic decision making as well.
Ezrin and CK18 (Montrer KRT18 Kits ELISA) 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 (Montrer VEGFA Kits ELISA) precedes AMPK (Montrer PRKAA1 Kits ELISA) and AKT (Montrer AKT1 Kits ELISA)-dependent phosphorylation of eNOSs1179 and production of NO.
high actin-ezrin intensity area restricts the lateral movement of B cell receptors upon stimulation, reducing receptor clustering and signaling
Ezrin may play a role in regulating lymphatic metastasis in hepatocellular carcinoma and might be inversely associated with A7 expression.
Augmented hypertension-induced glomerular capillary injury in mice lacking CLIC5 results from abrogation of Rac1-dependent Pak and ezrin activation, perhaps reducing the tensile strength of the podocyte actin cytoskeleton.
Data, including data from studies in knockout mice, suggest that VDR (vitamin D receptor) regulates expression of ezrin in enterocytes; VDR 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 (Montrer IL10 Kits ELISA) production by B cells
Merlin (Montrer NF2 Kits ELISA) 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 (Montrer EGFR Kits ELISA).
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 (Montrer CD44 Kits ELISA) clusters and the multimeric PIP2-CD44 (Montrer CD44 Kits ELISA)-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.
The cytoskeletal linker protein (Montrer LAT Kits ELISA) 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.
Data suggest that Mst4 phosphorylation of Thr545 of Acap4/Asap3 (Montrer ASAP3 Kits ELISA) in parietal cells leads to Acap4/Asap3 (Montrer ASAP3 Kits ELISA) binding to Ser66-phosphorylated ezrin (a cytoskeletal protein (Montrer ACTN1 Kits ELISA)); phosphorylation of Thr545 of Acap4/Asap3 (Montrer ASAP3 Kits ELISA) is required for relocation of H,K-ATPase (Montrer ATP1A1 Kits ELISA) to apical plasma membrane and acid secretion by parietal cells. (Mst4 = serine/threonine-protein kinase Mst4; Acap4/Asap3 (Montrer ASAP3 Kits ELISA) = GTPase-activating protein (Montrer RASA1 Kits ELISA) Acap4/Asap3 (Montrer ASAP3 Kits ELISA))
Spatial control of proton pump H,K-ATPase (Montrer ATP1A1 Kits ELISA) docking at the apical membrane by phosphorylation-coupled ezrin-syntaxin 3 (Montrer STX3 Kits ELISA) interaction.
1) NHE3 (Montrer SLC9A3 Kits ELISA) basal activity is regulated by a signaling complex that is controlled by sequential effects of two kinases, Akt (Montrer AKT1 Kits ELISA) and GSK-3 (Montrer GSK3b Kits ELISA), which act on a Ser (Montrer SIGLEC1 Kits ELISA) cluster in the same NHE3 (Montrer SLC9A3 Kits ELISA) 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