Abstract
Focal adhesions are highly dynamic multi-protein complexes found at the cell surface and effectively link the cell's internal cytoskeleton to a complex mixture of macromolecules known as the extracellular matrix and mediate transmission of signals from the extracellular matrix to the nucleus. Zyxin is one of the key focal adhesion proteins and is also found to shuttle in the nucleus. Although the mechanism of shuttling to the nucleus unclear, it moves out from the nucleus through a leucine-rich nuclear export signal sequence. It is known to contribute to fundamental cellular activities such as cell migration, adhesion and proliferation by interacting with a variety of cellular proteins. It is also linked with a number of cancers such as melanoma, hepatocellular carcinoma, oral squamous-cell carcinoma, Ewing sarcoma and prostate cancer. However, in many cases, the precise mechanisms by which the absence or presence of zyxin contributes to cancer progression or suppression is unknown. Thus, more work is required to gain insights into how zyxin modulates cellular functions in relationship to cancer. This review summarises the role of zyxin in cancer, with an emphasis on conflicting roles in prostate cancer.