Rabbit polyclonal antibody to VCL

Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development. Three structural vinculin domains include an amino~terminal head, a short, flexible proline~rich region and a carboxy~terminal tail . In the inactive state, the head and tail domains of vinculin interact to form a closed confirmation. The open and active form of vinculin translocates to focal adhesions where it is thought to be involved in anchoring F~actin to the membrane and regulation of cell migration. Phospholipid binding to the tail domain and subsequent phosphorylation of vinculin at Ser1033 and Ser1045 by PKC~α and Tyr100 and Tyr1065 by Src kinases weakens the head~tail interaction. This change in vinculin allows the binding of a number of other proteins, including talin, α~actinin and paxillin, which disrupts the head~tail interaction and initiates the conformational change from the inactive to active state. Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth. This is supported by a demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma.