MSN

Official Full Name

moesin

Organism

Homo sapiens

Gene ID

4478

Background

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. [provided by RefSeq, Jul 2008]

Synonyms

HEL70; IMD50

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CDCB194638	Rabbit MSN ORF clone (XM_008272722.1)	Inquiry
CDCL134655	Human Msn ORF clone (NM_010833.2)	Inquiry
CDCR283100	Human MSN ORF Clone(NM_002444.2)	Inquiry
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CDCS410800	Human MSN ORF Clone (BC017293)	Inquiry

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CC-896	MSN Easy KO Kit	Inquiry

Detailed Information

The membrane protein (moesin) is a membrane cytoskeletal connexin and is a member of the ERM family of ezrin/radixin/moesin. Moesin is present in a variety of cells, including vascular endothelial cells, and does not function biologically when it is not activated. Various extracellular signal stimulating factors can cause changes in the conformation of moesin molecules, thereby activating moesin, which activates moesin to play an important role in cell surface structure formation, cell junction, cell shape maintenance, cell growth, migration, mitosis, and membrane trafficking. It also participates in the regulation of various biological functions of cells by regulating cellular signaling pathways. Moesin, which is activated by various inflammatory cytokines, is involved in vascular endothelial cell injury by regulating cell adhesion, altering the cytoskeleton, and increasing cell permeability.

Figure 1. In the nucleus Moesin participates in mRNA export.( Kristó, et al. 2017)

Physiological Function of MSN

Maintaining normal cell polarity is a prerequisite for cell morphogenesis, and abnormal expression of ERM proteins can affect the establishment of cell polarity. The study found that only the expression of moesin in Drosophila is an ideal model for studying the function of ERM protein. Drosophila, which lacks moesin expression, has reduced fibronectin (F-actin) in the top of the columnar epithelium in the organ bud. The basal polarity disappears and actin aggregates ectopically within the cell, generally showing a lethal phenotype. Studies have shown that inhibition of moesin/radixin expression in cultured primary neuronal cells can inhibit the formation of growth cones and axons. Studies on Hela cells cultured outside the body revealed that during the proliferation and division of Hoa cells, the phosphorylation of ERM protein in the cleavage sulcus increased significantly and participated in the cytokinesis process. Studies have also found that meningococcal meningositis can cause vascular endothelial cells (VECs) cultured in vitro to form ezrin-rich and moesin-containing pro-trusion-mediated mutations that mediate endocytosis of VEC.

Relationship between Moesin and Vascular Endothelial Cell Injury

Tumor necrosis factor-α (TNF-α) is a major regulator of inflammatory response in VEC injury. It has a dual biological effect. It participates in the fight against bacterial, viral and parasitic infections at low concentrations, promotes tissue repair and regulates inflammation. In the reaction, when a large amount of TNF-α is produced and released in a large amount in the body, the immune balance of the body is destroyed, and various pathological damages are produced together with other inflammatory factors.

McKenzie et al through skin cell study found within human pulmonary capillary blood vessels, TNF-α by activation of p38MAPK, PKC subunits and PIPSKIa signal passage so obtained moesin phosphorylation is activated, and moesin worked as a downstream target of the signaling pathway. Moesin is activated to induce the increase and the permeability of the skin disease cells intravascular cell skeleton. However, the mechanism by which moesin causes cytoskeletal changes and permeability increase of vascular endothelial cells is not clear. It is speculated that it may be related to the following two aspects: first, moesin directly promotes the depolymerization reaction of F-actin; second, moesin works by regulating some of the necessary intermediate regulatory factors such as focalin-hesionkinase and RhoGTPase in signaling pathways that mediate cytoskeletal changes and increased permeability.

References:

Kristó, Ildikó, Bajusz, C. , Borsos, B. N. , Pankotai, T. , Dopie, J. , & Jankovics, F. , et al. (2017). The actin binding cytoskeletal protein moesin is involved in nuclear mrna export. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, S0167488917301453.
Ansa-Addo, E. A. , Zhang, Y. , Yang, Y. , Hussey, G. S. , & Li, Z. . (2017). Membrane-organizing protein moesin controls treg differentiation and antitumor immunity via tgf-? signaling. Journal of Clinical Investigation, 127(4), 1321.
Kawaguchi, K. , Yoshida, S. , Hatano, R. , & Asano, S. . (2017). Pathophysiological roles of ezrin/radixin/moesin proteins. Biological & Pharmaceutical Bulletin, 40(4), 381-390.

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