Moesin (MSN)

Membrane-Organizing Extension Spike Protein

SPN	U209
HGNC	7373
MGI	97167
PubMed	22433855
RGD	621260
UniProt	P26038
Wiki	Moesin

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 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.which represents a single 4.2-kb mRNA encoding a protein of 577 amino acids. It contains no apparent signal peptide or transmembrane domain.

Reference

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"Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family."
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"ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1."
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"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain."
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"The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation."
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