Vinculin, a cytoskeletal protein, plays an important role during embryonic development and focal adhesion regulation. There are three domains of structural vinculin, an amino-terminal head and a proline-rich, short region, and a carboxy terminal tail. The closed confirmation is formed when the head domain and tail domains interact in the inactive state.
Anti-Vinculin/VCL antibody is active and open form translocates to focal adhesions, where it is believed to play a role in the anchoring of F-actin to membrane and regulation cell migration. Phospholipid binding at the tail domain and subsequent PKC-a and Tyr100/Tyr1065 phosphorylation (Ser1033 and Ser1045 respectively) weakens the head–tail interaction.
This alteration in vinculin permits the binding of a variety of proteins, such as talin and a-actinin, which causes the head-tail interaction to be disrupted and the conformational transition from inactive to active. Vinculin deficiencies can lead to a decrease of cell adhesion and increased cell motility. This could be a role in metastatic growth.
This observation is supported by the evidence of a relationship between reduced vinculin expression, increased carcinogenesis, and metastasis for colorectal carcinoma. Vinculin (VCL), a cytoskeletal protein, is associated with cell cell and cell-extracellular matrix adherens type junctions. It is one of many interacting proteins that anchor F-actin to membranes.
A sequence of molecular interactions may be involved in transmembrane adhesion plaque assembly. The adhesion plaque assembly is facilitated by talin binding to the beta subunit (integrin) Talin binds with vinculin, which interacts with alpha -actinin, and possibly with itself.