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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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detection of Ezrin and E-cadherin expression in cervical smears, could be a potential prognostic marker for identifying cervical lesions with high-risk of progression to invasive cervical cancer, and may help on the selection of an appropriate therapy or avoid unnecessary treatment
Ezrin and myosin II play critical roles in enhancing line tension by promoting the formation of an actomyosin ring.
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 to enhance gap junction assembly, communication, and cell fusion.
High Ezrin expression is associated with osteosarcoma.
L1CAM promotes esophageal squamous cell carcinoma tumorigenicity by upregulating ezrin expression.
This is the first study to verify the relationship of the expression of RhoA and Ezrin proteins in vaginal tissue of Postmenopausal atrophic vagina.
ezrin facilitates AQP2 endocytosis, thus linking the dynamic actin cytoskeleton network with AQP2 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 drives Ras activity and tumorigenesis in melanomas in a two-fold way; inactivation of the tumor suppressor merlin and activation of the growth promoting ERM family.
Data suggest that EGF induces colorectal cancer cells to undergo epithelial-mesenchymal transition, enhances their ability to invade/migrate, and promotes phosphorylation of Ezrin at Tyr353. (EGF = epidermal growth factor)
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.
The expression pattern and subcellular localization of ezrin and moesin 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
The results reveal a supportive role of ERMs in cortical activities during cytokinesis, and also provide insight into the selective mechanism that preferentially associates cytokinesis-relevant proteins with the division site.
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.
Data suggest that Mst4 phosphorylation of Thr545 of Acap4/Asap3 in parietal cells leads to Acap4/Asap3 binding to Ser66-phosphorylated ezrin (a cytoskeletal protein); phosphorylation of Thr545 of Acap4/Asap3 is required for relocation of H,K-ATPase to apical plasma membrane and acid secretion by parietal cells. (Mst4 = serine/threonine-protein kinase Mst4; Acap4/Asap3 = GTPase-activating protein Acap4/Asap3)
Spatial control of proton pump H,K-ATPase docking at the apical membrane by phosphorylation-coupled ezrin-syntaxin 3 interaction.
1) NHE3 basal activity is regulated by a signaling complex that is controlled by sequential effects of two kinases, Akt and GSK-3, which act on a Ser cluster in the same NHE3 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 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 precedes AMPK and AKT-dependent phosphorylation of eNOSs1179 and production of NO.
The cytoskeletal linker protein 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, a bipartite guanine nucleotide exchange factor complex for the small GTPase 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