Ezrin, also known as cytovillin or villin-2, is a protein that in humans is encoded by the EZR gene.
Structure
The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contains an ERM domain.
Function
The cytoplasmic peripheral protein encoded by this gene can be phosphorylated by protein-tyrosine kinase in microvilli and is a member of the ERM protein family. This protein serves as a linker between plasma membrane and actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization.
The N-terminus domain (also called FERM domain) binds sodium-hydrogen exchanger regulatory factor (NHERF) protein (involving long-range allostery). This binding can happen only when ezrin is in its active state. The activation of ezrin occurs in synergism of the two factors: binding of the N-terminus domain to phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphorylation of threonine T567 in the C-terminus domain. Binding to actin filaments (via C-terminus) and to membrane proteins (via N-terminus) stabilizes the protein's conformation in its active mode. The membrane proteins like CD44 and ICAM-2 are indirect binding partners of ezrin, while EBP50 (ERM binding protein 50) can associate with ezrin directly.
Interactions VIL2 has been shown to interact with:
CD43, FASLG, ICAM-1, ICAM2, ICAM3, Merlin, MSN, PIK3R1, PALLD S100P, SDC2, SLC9A3R1, SLC9A3R2, and VCAM-1.
References
Further reading