Moesin

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Protein-coding gene in the species Homo sapiens

title: "Moesin" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["human-proteins"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/human-proteins" source: "https://en.wikipedia.org/wiki/Moesin" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Moesin is a protein that in humans is encoded by the MSN gene.

Moesin (for membrane-organizing extension spike protein) is a member of the ERM protein 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.

Moesin has FERM domain at N-terminal.

Interactions

Moesin has been shown to interact with:

References

References

  1. (Oct 1991). "Moesin: a member of the protein 4.1-talin-ezrin family of proteins". Proc. Natl. Acad. Sci. U.S.A..
  2. (Sep 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..
  3. "Entrez Gene: MSN moesin".
  4. (Jun 1998). "CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts". Blood.
  5. (Feb 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..
  6. (Sep 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..
  7. (Mar 2002). "A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting". J. Biol. Chem..
  8. (Nov 2001). "The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain". Biochem. Biophys. Res. Commun..
  9. (Jun 2002). "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes". J. Cell Biol..
  10. (Mar 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem..
  11. (Aug 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.
  12. (Nov 1993). "Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins". Proc. Natl. Acad. Sci. U.S.A..

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human-proteins