Ezrin

"Cvl" redirects here. For other uses, see CVL.

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-terminal 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: 1) binding of the N-terminal domain to phosphatidylinositol(4,5)bis-phosphate (PIP2) and 2) phosphorylation of threonine T567 in the C-terminal domain. Binding to actin filaments (via C-terminal) and to membrane proteins (via N-terminal) 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.