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Human MSN Protein expressed in HEK-293 Cells - ABIN2726221
Miyaji, Shahrizaila, Umapathi, Chan, Hirata, Yuki: Are ERM (ezrin/radixin/moesin) proteins targets for autoantibodies in demyelinating neuropathies? in Human immunology 2015
The distribution of Moesin in the nucleus suggests a function in transcription and the depletion of mRNA export factors Nup98 (show NUP98 Proteins) or its interacting partner, Rae1 (show RAE1 Proteins), leads to the nuclear accumulation of Moesin, suggesting that the nuclear function of the protein is linked to mRNA export
Data show that Moesin upregulation influences extra-centrosome behavior and robust bipolar spindle formation.
Btsz and Moesin guide luminal membrane morphogenesis through organizing actin.
The conserved C-terminal coiled-coil domain of Slik, which is necessary and sufficient for apical localization of the kinase in epithelial cells, is not required for Moesin phosphorylation but is critical for the growth-promoting function of Slik.
Early endocytosis maintains normal steady-state levels of Crumbs, which recruits apical phosphorylated (active) Moesin, which in turn regulates seamless tube shape through modulation of cortical actin filaments.
Moesin interacts with an unusual RhoGAP (show ARHGAP1 Proteins), Conundrum (Conu), and recruits it to the cell cortex to negatively regulate RhoA (show RHOA Proteins) activity.
Moesin stabilizes microtubules via a direct interaction at the cell cortex.
Wgn-Moe signaling cascade plays a key role in photoreceptor target field innervations through cell autonomous and non-cell autonomous mechanisms.
Drosophila melanogaster protein phosphatase type 1 beta (flapwing) co-regulates dephosphorylation and altered activity of both Merlin (show NF2 Proteins) and Moesin.
This study revealed a novel mechanism for controlling salivary gland lumen size, namely through Rho1-dependent actin (show ACTB Proteins) polymerization and distribution and downregulation of apical phosphorylated moesin.
suggest that Ve-cadherin (show CDH5 Proteins) and Moesin1 function to establish and maintain apical/basal polarity during multicellular lumen formation in the intersegmental vessels
results suggest a new role for moesin, acting in a signalling pathway facilitating the differentiation of extraembryonic endoderm
The Ano1 (show ANO1 Proteins)-moesin interaction limits Ano1 (show ANO1 Proteins) lateral membrane mobility and contributes to microvilli scaffolding, therefore stabilizing larger membrane structures. Collectively, these results reveal a newly identified role for Ano1 (show ANO1 Proteins) in shaping the plasma membrane during oogenesis, with broad implications for the regulation of microvilli in epithelia.
This review focuses on the role of moesin in microvascular permeability and angiogenesis, and on the involvement of Src (show SRC Proteins) and ROS (show ROS1 Proteins) in endothelial barrier disruption.
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.
The authors demonstrated that the expression of MSN in glioma specimens were negatively correlated with miR (show MLXIP Proteins)-200c expression, and MSN overexpression rescued the phenotype about cell proliferation and invasion induced by miR (show MLXIP Proteins)-200c.
The expression pattern and subcellular localization of ezrin (show EZR Proteins) and moesin correlate with clinicopathological variables such as patients' age, tumor grade and hormonal status.
Moesin and merlin (show NF2 Proteins) regulate urokinase receptor-dependent endothelial cell migration, adhesion and angiogenesis
These results indicate that loss of miR (show MLXIP Proteins)-200c, as a consequence of p53 (show TP53 Proteins) mutation, can upregulate Moesin oncogene (show RAB1A Proteins) and thus promote carcinogenesis in breast cancer
the administration of 10(-6) M retinoic acid (10-20 min) induces the activation of the migration-related proteins Moesin, FAK (show PTK2 Proteins), and Paxillin (show PXN Proteins) in T-47D breast cancer cells.
Up-regulation of moesin expression in glioblastoma cells correlated with increases in cell proliferation, invasion and migration, suggesting moesin's role in glioblastoma progression.
this study identifies X-linked primary immunodeficiency associated with hemizygous mutations in the moesin gene
These results of this study may pave the way for exploiting moesin as a novel target for intervention in muscular dystrophy.
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 proteins and increased Rho-GTP (show AK3 Proteins).
Collectively, these results implicate both moesin and myosin IIA in the regulation of phagolysosome biogenesis and in host defense against infections.
these findings underscore the importance of moesin in IL-15 (show IL15 Proteins)-dependent CD8 (show CD8A Proteins)+ Treg cell homeostasis and the control of self-tolerance
Moesin is an important regulator of the surface abundance and stability of TbetaRII and is important in facilitating the efficient generation of iTregs.
The expression of moesin was upregulated in cardiomyocytes under inflammation, inducing protrusion formation in a phosphorylation-dependent fashion.
this study shows that low neutrophil rolling in inflamed venules was impaired in moesin-deficient mice
High blood moesin levels were also observed in cecal ligation and puncture (CLP)-induced sepsis in mice. Administration of blocking moesin antibodies attenuated CLP-induced septic death.
An increase in moesin expression may contribute to the increased expression of P-gp (show ABCB4 Proteins) in blood brain barrier endothelial cells, leading to the development of morphine analgesic tolerance.
phosphorylation-regulated (show PHAX Proteins) interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein (show PFN1 Proteins) moesin
Moesin (for membrane-organizing extension spike protein) is a member of the ERM family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons. Moesin is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement.
, membrane-organizing extension spike protein