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Human EZR Protein expressed in HEK-293 Cells - ABIN2720647
Miyaji, Shahrizaila, Umapathi, Chan, Hirata, Yuki: Are ERM (ezrin/radixin/moesin) proteins targets for autoantibodies in demyelinating neuropathies? in Human immunology 2015
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these findings suggest that baicalein inhibits the proliferation, migration and invasion and induces apoptosis in Osteosarcoma (OS) cells by activating the miR183/Ezrin pathway, revealing a novel mechanism underlying antiOS effects of baicalein.
Ezrin-anchored PKA phosphorylates serine 369 and 373 on connexin 43 (show GJA1 Proteins) to enhance gap junction assembly, communication, and cell fusion.
High Ezrin expression is associated with osteosarcoma.
L1CAM (show L1CAM Proteins) promotes esophageal squamous cell carcinoma tumorigenicity by upregulating ezrin expression.
This is the first study to verify the relationship of the expression of RhoA (show RHOA Proteins) and Ezrin proteins in vaginal tissue of Postmenopausal atrophic vagina.
ezrin facilitates AQP2 (show AQP2 Proteins) endocytosis, thus linking the dynamic actin cytoskeleton network with AQP2 (show AQP2 Proteins) trafficking.
FUT4/LeY was critical to the TAMs-mediated EMT; this process might be associated with the up-regulation of Ezrin phosphorylation by FUT4/LeY-mediated fucosylation
CPI-17 (show PPP1R14A Proteins) drives Ras activity and tumorigenesis in melanomas in a two-fold way; inactivation of the tumor suppressor merlin (show NF2 Proteins) and activation of the growth promoting ERM (show ETV5 Proteins) family.
Data suggest that EGF (show EGF Proteins) induces colorectal cancer cells to undergo epithelial-mesenchymal transition, enhances their ability to invade/migrate, and promotes phosphorylation of Ezrin at Tyr353. (EGF (show EGF Proteins) = epidermal growth factor (show EGF Proteins))
Binding of phosphatidylinositol 4,5-biphosphate to ezrin induces a conformational change permitting the insertion of the LOK C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue.
Data suggest that Mst4 (show MST4 Proteins) phosphorylation of Thr545 of Acap4/Asap3 (show ASAP3 Proteins) in parietal cells leads to Acap4/Asap3 (show ASAP3 Proteins) binding to Ser66-phosphorylated ezrin (a cytoskeletal protein (show ACTN1 Proteins)); phosphorylation of Thr545 of Acap4/Asap3 (show ASAP3 Proteins) is required for relocation of H,K-ATPase (show ATP1A1 Proteins) to apical plasma membrane and acid secretion by parietal cells. (Mst4 (show MST4 Proteins) = serine/threonine-protein kinase Mst4 (show MST4 Proteins); Acap4/Asap3 (show ASAP3 Proteins) = GTPase-activating protein (show RASA1 Proteins) Acap4/Asap3 (show ASAP3 Proteins))
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).
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.
Ezrin level may serve as a differential diagnostic and/or prognostic biomarker for high and low lymphatic metastasis -Hepatocellular carcinoma (HCC (show FAM126A Proteins))and may be beneficial in the diagnosis of HCC (show FAM126A Proteins) disease
Inactivation of SHIP2 (show INPPL1 Proteins) leads to increased microvilli formation and solute reabsorption by the renal proximal tubule and was associated with hyperactivated ezrin/radixin/moesin (show MSN Proteins) proteins and increased Rho-GTP (show AK3 Proteins).
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 (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
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.
ELMO-DOCK1 (show DOCK1 Proteins), a bipartite guanine nucleotide exchange factor (show ARHGEF12 Proteins) complex for the small GTPase (show RACGAP1 Proteins) Rac1, and for the membrane-cytoskeletal linker Ezrin, regulates centriole/basal body migration, docking and spacing.
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)
, villin 2
, ezrin L homeolog
, ezrin S homeolog