Moesin (membrane-organizing extension spike protein) was initially isolated from bovine uterus in 1988. It was first identified as a heparin-binding protein and thought to be extracellular (Lankes et al. 1988), but later shown to be intracellular (Lankes and Furthmayr 1991). Moesin belongs to the ERM family of proteins (ezrin, radixin, and moesin), a subclass of the large protein 4.1 superfamily that also includes protein 4.1, talin and merlin. The ERM family of proteins is credited with coupling filamentous actin to the cell membrane and has roles in numerous cellular processes involving modification of the cortical actin network in conjunction with the plasma membrane.
Distribution and Cell Biology
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- Liu X, Yang T, Suzuki K, Tsukita S, Ishii M, Zhou S, Wang G, Cao L, Qian F, Taylor S, Oh MJ, Levitan I, Ye RD, Carnegie GK, Zhao Y, Malik AB, Xu J. Moesin and myosin phosphatase confine neutrophil orientation in a chemotactic gradient. J Exp Med. 2015;212:267–80. doi:10.1084/jem.20140508.CrossRefPubMedPubMedCentralGoogle Scholar