The recent discovery of the 3D structure[citation needed] sheds light on how this protein tailors its shape to perform a variety of functions.

Vinculin is associated with focal adhesion and adherens junctions, resulting in significant protein dynamics[citation needed].

[8] The complex at the focal adhesions consists of several proteins such as vinculin, α-actinin, paxillin, and talin, at the intracellular face of the plasma membrane.

The complex then serves to anchor actin filaments to the membrane and thus, helps to reinforce force on talin within the focal adhesions.

[7] It was discovered that cells that are deficient in vinculin have growth cones that advance more slowly, as well as filopodia and lamellipodia that were less stable than the wild-type.

[9] Vinculin's ability to interact with integrins to the cytoskeleton at the focal adhesion appears to be critical for control of cytoskeletal mechanics, cell spreading, and lamellipodia formation.

Thus, vinculin appears to play a key role in shape control based on its ability to modulate focal adhesion structure and function.

When vinculin resides in its inactive form, the protein is kept designated to the cytoplasm unlike the focal adhesion points bound from the active state.

The hydrophobic residues that define the VBS are themselves 'masked' and are buried in the core of a series of helical bundles that make up the talin rod.

[15] Compared metavinculin sequences from pig, man, chicken, and frog, and found the insert to be bipartite: the first part variable and the second highly conserved.