Ezrin is a key member of the Ezrin-Radixin-Moesin (ERM) protein family, functioning as a linker protein that connects the plasma membrane to the actin cytoskeleton. It plays a crucial role in mediating membrane-cytoskeleton interactions, regulating cell morphology, adhesion, migration, and survival. Structurally, Ezrin consists of three main domains: an N-terminal FERM domain that binds to membrane proteins and lipids, a central helical linker region, and a C-terminal ERM-associated domain (C-ERMAD) that interacts with actin filaments. In its inactive state, Ezrin is held in the cytoplasm through intramolecular interactions, but it can be activated by phosphorylation at Thr567, leading to its translocation to the plasma membrane. Ezrin is essential for various cellular functions, including the formation of membrane protrusions like microvilli and invadopodia, which are critical for cell motility and invasion. Abnormal regulation of Ezrin has been implicated in several diseases, particularly cancer, where its overexpression or dysregulation can promote tumor progression, invasion, and metastasis.
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