Moesin

From Wikipedia, the free encyclopedia

Moesin

PDB rendering based on 1e5w.

Available structures: 1e5w, 1ef1, 1j19, 1sgh, 2d10, 2d11, 2d2q, 2yvc

Identifiers

Symbol(s)

MSN;

External IDs

OMIM: 309845 MGI: 97167 HomoloGene: 1833

Gene ontology
Molecular Function:	• receptor binding • structural constituent of cytoskeleton • cytoskeletal protein binding
Cellular Component:	• uropod • cytoplasm • cytoskeleton • plasma membrane • basolateral plasma membrane • apical plasma membrane
Biological Process:	• cell motility

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002444 (mRNA)
NP_002435 (protein)

NM_010833 (mRNA)
NP_034963 (protein)

Location

Chr X: 64.8 - 64.88 Mb

Chr X: 92.34 - 92.37 Mb

Pubmed search

[1]

[2]

Moesin, also known as MSN, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: MSN moesin.

[edit] Further reading

Tsukita S, Yonemura S (1997). "ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction.". Curr. Opin. Cell Biol. 9 (1): 70–5. PMID 9013673.
Vaheri A, Carpén O, Heiska L, et al. (1997). "The ezrin protein family: membrane-cytoskeleton interactions and disease associations.". Curr. Opin. Cell Biol. 9 (5): 659–66. PMID 9330869.
Matarrese P, Malorni W (2006). "Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death.". Cell Death Differ. 12 Suppl 1: 932–41. doi:10.1038/sj.cdd.4401582. PMID 15818415.
Lankes WT, Furthmayr H (1991). "Moesin: a member of the protein 4.1-talin-ezrin family of proteins.". Proc. Natl. Acad. Sci. U.S.A. 88 (19): 8297–301. PMID 1924289.
Gary R, Bretscher A (1995). "Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site.". Mol. Biol. Cell 6 (8): 1061–75. PMID 7579708.
Schwartz-Albiez R, Merling A, Spring H, et al. (1995). "Differential expression of the microspike-associated protein moesin in human tissues.". Eur. J. Cell Biol. 67 (3): 189–98. PMID 7588875.
Amieva MR, Furthmayr H (1995). "Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts.". Exp. Cell Res. 219 (1): 180–96. doi:10.1006/excr.1995.1218. PMID 7628534.
Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, et al. (1995). "Physical association of moesin and CD46 as a receptor complex for measles virus.". J. Virol. 69 (4): 2248–56. PMID 7884872.
Wilgenbus KK, Hsieh CL, Lankes WT, et al. (1994). "Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN).". Genomics 19 (2): 326–33. doi:10.1006/geno.1994.1065. PMID 8188263.
Gary R, Bretscher A (1993). "Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins.". Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10846–50. PMID 8248180.
Dunster LM, Schneider-Schaulies J, Löffler S, et al. (1994). "Moesin: a cell membrane protein linked with susceptibility to measles virus infection.". Virology 198 (1): 265–74. PMID 8259662.
Nakamura F, Amieva MR, Furthmayr H (1996). "Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets.". J. Biol. Chem. 270 (52): 31377–85. PMID 8537411.
Ott DE, Coren LV, Kane BP, et al. (1996). "Cytoskeletal proteins inside human immunodeficiency virus type 1 virions.". J. Virol. 70 (11): 7734–43. PMID 8892894.
Hecker C, Weise C, Schneider-Schaulies J, et al. (1997). "Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin.". Virus Res. 49 (2): 215–23. PMID 9213396.
Serrador JM, Alonso-Lebrero JL, del Pozo MA, et al. (1997). "Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization.". J. Cell Biol. 138 (6): 1409–23. PMID 9298994.
Reczek D, Berryman M, Bretscher A (1998). "Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family.". J. Cell Biol. 139 (1): 169–79. PMID 9314537.
Murthy A, Gonzalez-Agosti C, Cordero E, et al. (1998). "NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins.". J. Biol. Chem. 273 (3): 1273–6. PMID 9430655.
Yonemura S, Hirao M, Doi Y, et al. (1998). "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2.". J. Cell Biol. 140 (4): 885–95. PMID 9472040.