Disease relevance of Msn

• Galpha13 activation rescues moesin-depletion induced apoptosis in F9 teratocarcinoma cells [1].

High impact information on Msn

• Cerebellar long-term synaptic depression requires PKC-mediated activation of CPI-17, a myosin/moesin phosphatase inhibitor [2].
• Ezrin protein levels in Vil2(kd/kd) stomachs decreased to <5% of the wild-type levels without compensatory up-regulation of radixin or moesin [3].
• Involvement of ezrin/moesin in de novo actin assembly on phagosomal membranes [4].
• In sharp contrast, moesin antisense PONs did not singly affect cell-cell and cell-substrate adhesion, whereas it partly affected the microvilli structures [5].
• The active role of ERMs was further confirmed by double transfections with the N-terminal domain of moesin, which acts as a dominant negative form of ERMs, and was able to delocalize EWIs from the uropod of polarized leukocytes [6].

Biological context of Msn

• The murine Msn locus was mapped to the X chromosome as well by studying a rodent x mouse hybrid panel [7].
• CONCLUSION: These changes in proximal Na/Pi cotransport may involve a signal transduction cascade including PDZ-dc1, ezrin, moesin, our phosphoprotein, and possibly other proteins [8].
• Experiments with full-length and truncated bacterial fusion proteins localized the actin-binding site in moesin to the extreme carboxy terminus, a highly conserved sequence [9].
• Furthermore, morpholino antisense and shRNA approaches show that moesin expression is essential since its knockdown leads to altered F-actin distribution and subsequent apoptosis [1].
• Our study demonstrates a link between Galpha13 signaling that regulates differentiation of F9 cells through primitive to parietal endoderm and a moesin requirement for cell survival [1].

Anatomical context of Msn

• A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites [10].
• Moesin was present in the apical membrane of all undifferentiated epithelial cells [11].
• However, in differentiated cells, ezrin and moesin were selectively localized to apical membranes of ciliated airway cells and were absent from secretory cells [11].
• To assess the possible unique functions of ERM proteins in vivo, the moesin gene located on the X chromosome was disrupted by gene targeting in embryonic stem cells [12].
• The expression of moesin was modestly higher at the mural trophectoderm of implantation-competent blastocysts, while the localization appeared to be present primarily on the polar trophectoderm cell surface of Day 4 blastocysts [13].

Associations of Msn with chemical compounds

• Moesin was coprecipitated with glutathione S-transferase-fusion proteins of the l-gicerin cytoplasmic domain but not with the s-gicerin cytoplasmic domain [14].
• Stress fibers and microextensions of DOTMAC-extracted cells were readily stained with anti-beta-actin antibodies, and antibodies to vinculin and moesin stained focal contacts and microextensions, respectively [15].

Other interactions of Msn

• Ezrin, moesin, and PDZ-dc1 protein levels were not increased following short term VE [8].
• In the receptive uterus on Day 4 of pregnancy, ERM proteins were localized to the uterine epithelium, while on Day 5 the localization, especially of radixin and moesin, extended to the stroma surrounding the implantation chamber [13].
• When cells were double-stained with antibodies to gicerin and moesin, a microvilli-specific protein, the staining of l-gicerin corresponded to that of moesin in the elongated microvilli [14].
• This requires a dynamic actin cytoskeleton, moesin, components of Rho-mediated signal pathways, rearrangement of membrane constituents and the formation of focal adhesion sites [16].

Analytical, diagnostic and therapeutic context of Msn

• Based on Western and immunoprecipitation data for ezrin, moesin, and PDZ-dc1 we believe that it is unlikely that our phosphoprotein is any of these 3 proteins [8].
• Immunofluorescence micrographs of permeabilized cells and cell "footprints" showed moesin co-localization with actin at the cytoplasmic surface of the plasma membrane, consistent with a role as a membrane-actin-linking protein [9].

References