Ena/Vasp homology proteins

Overview

Crystal structure of an Ena/VASP homology protein.

Ena/VASP homology proteins are a family of proteins involved in the regulation of the actin cytoskeleton. These proteins play a crucial role in cell movement, adhesion, and shape by promoting the assembly of actin filaments. They are characterized by the presence of an Ena/VASP homology (EVH) domain, which is essential for their function in actin dynamics.

Structure

Ena/VASP proteins typically contain several conserved domains:

• EVH1 domain: This domain is responsible for binding to proline-rich sequences in other proteins, facilitating interactions with various signaling molecules.
• Proline-rich region: This region serves as a binding site for SH3 and WW domain-containing proteins, which are involved in signal transduction pathways.
• EVH2 domain: This domain is crucial for actin binding and filament elongation. It contains a G-actin binding site and a F-actin binding site, which are essential for actin polymerization.

Function

Ena/VASP proteins are involved in several cellular processes, including:

• Actin polymerization: They promote the elongation of actin filaments by protecting the growing ends from capping proteins.
• Cell motility: By regulating actin dynamics, Ena/VASP proteins facilitate cell movement, which is essential for processes such as embryonic development and wound healing.
• Cell adhesion: These proteins are involved in the formation of focal adhesions, which are contact points between the cell and the extracellular matrix.

Clinical Significance

Dysregulation of Ena/VASP proteins has been implicated in various diseases, including cancer and cardiovascular disorders. Their role in cell motility and adhesion makes them potential targets for therapeutic intervention in metastatic cancer.

Related Pages

• Actin
• Cytoskeleton
• Cell motility
• Signal transduction