Moesin Protein, Human (His)

Moesin, an Ezrin-radixin-moesin (ERM) family protein, serves as a crucial link between the actin cytoskeleton and the plasma membrane, thereby influencing the structure and function of specific domains in the cell cortex. Functioning as a tether for actin filaments, Moesin undergoes oscillation between a resting and an activated state, establishing transient interactions with the actin cytoskeleton. Upon phosphorylation of its C-terminal threonine, Moesin becomes activated, leading to interactions with F-actin and subsequent cytoskeletal rearrangements. These rearrangements play a pivotal role in regulating various cellular processes, including cell shape determination, membrane transport, and signal transduction. Moesin's significance is particularly pronounced in immunity, impacting both T and B-cell homeostasis and self-tolerance, and regulating lymphocyte egress from lymphoid organs. Additionally, Moesin modulates phagolysosomal biogenesis in macrophages and participates in immunologic synapse formation. The protein adopts a closed conformation (inactive form) through a head-to-tail association of its N-terminal and C-terminal halves, rendering it incapable of actin or membrane-binding in this state.