Moesin (MSN)
The protein contains 577 amino acids for an estimated molecular weight of 67820 Da.
Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation (PubMed:27405666). (updated: May 8, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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| Variant | Description |
|---|---|
| IMD50 |
Biological Process
Cellular response to testosterone stimulus
Establishment of endothelial barrier
Establishment of epithelial cell apical/basal polarity
Gland morphogenesis
Immunological synapse formation
Interleukin-12-mediated signaling pathway
Leukocyte cell-cell adhesion
Leukocyte migration
Membrane to membrane docking
Movement of cell or subcellular component
Positive regulation of cellular protein catabolic process
Positive regulation of early endosome to late endosome transport
Positive regulation of gene expression
Positive regulation of podosome assembly
Positive regulation of protein localization to early endosome
Regulation of cell shape
Regulation of cell size
Regulation of lymphocyte migration
Regulation of organelle assembly
T cell aggregation
T cell migration
T cell proliferation
Viral process
Cellular Component
Apical part of cell
Apical plasma membrane
Basolateral plasma membrane
Blood microparticle
Cell periphery
Cell surface
Cytoplasm
Cytoskeleton
Cytosol
Extracellular exosome
Extracellular space
Extrinsic component of membrane
Filopodium
Focal adhesion
Invadopodium
Microvillus
Microvillus membrane
Myelin sheath
Nucleus
Perinuclear region of cytoplasm
Plasma membrane
Pseudopodium
Uropod
Vesicle
The reference OMIM entry for this protein is 309845
Moesin; msn
Membrane-organizing extension spike protein
CLONING
Lankes et al. (1988) isolated from bovine uterus a protein that is a candidate receptor for heparin or heparan sulfate in the interaction of basement membrane heparan sulfate and cells. They called the protein moesin (for membrane-organizing extension spike protein). Further studies indicated a significant homology in sequence to ezrin (123900), protein 4.1 (130500), talin (186745), radixin (179410), and merlin (607379). These proteins constitute a family with structural and probably functional relationships; all of them are localized to the submembranous cytoskeleton. Moesin is widely expressed in different tissues in cells, where it is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement. Lankes and Furthmayr (1991) cloned and sequenced the complete cDNA of moesin, which represents a single 4.2-kb mRNA encoding a protein of 577 amino acids. It contains no apparent signal peptide or transmembrane domain.GENE FUNCTION
The immunologic synapse is the T cell-APC (antigen-presenting cell) contact site where T-cell receptors (TCRs), coreceptors, signaling molecules, and adhesion receptors polarize upon antigen recognition. The formation of the immunologic synapse is thought to be important for receptor signal transduction and full T-lymphocyte activation. CD43 (182160) is a large sialoprotein diffusely expressed in unactivated T cells. Using antigen-activated T cells and confocal microscopy, Delon et al. (2001) demonstrated that moesin is excluded from the region of T cell-APC contact and colocalizes with CD43. Western blot and immunocytochemical analyses showed that moesin is rapidly dephosphorylated upon antigen recognition and then rephosphorylated on threonine residues. Only phosphorylated moesin was able to bind CD43. Delon et al. (2001) concluded that T-cell activation requires the removal of CD43 from the immunologic synapse to allow efficient engagement of the TCR with molecules on the APC. Using mouse helper T cell lines and confocal microscopy, Allenspach et al. (2001) determined that the cytoplasmic tail of CD43 is necessary and sufficient for CD43 removal from the immunologic synapse. In at least some cells, CD43 is located at the distal pole of the T cell together with ezrin and moesin. No differences in the behavior of ezrin and moesin were noted throughout the study. Using cells from Cd43 -/- mice, Allenspach et al. (2001) observed that ezrin-radixin-moesin (ERM) family proteins move independently of the large CD43 mucin. Overexpression of a dominant-negative ERM mutant containing the N-terminal 320 amino acids of ezrin inhibited the activation-induced movement of CD43 without affecting conjugate formation. The dominant-negative mutant reduced cytokine production but not the expression of T-cell activation markers. Speck et al. (2003) showed that the sole Drosophila ERM protein moesin promotes cortical actin assembly and apical-basal polarity. As a result, cells lacking moesin lose epithelial characteristics and adopt invasive migratory behavior. Speck et al. (2003) concluded that moesin facilitates epithelial morphology not by providing an essential structural function, but rather by antagonizing activity of the small GTPase Rho (RHOA; 165390). Thus, moesin functions in maintaining epithelial integrity by regulating cell-signaling events that affect actin organization and polarity. Furthermore, Speck et al. (2003 ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
May 11, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 309845 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed