The interaction between two proteins, Focal adhesion kinase (FAK) and Myosin-1E (MYO1E), may help cancer cells grow and metastasize, according to a study led by researchers from Mayo Clinic, University of Tuebingen, and University of Copenhagen. FAK has been studied intensely. It is a nonreceptor tyrosine kinase involved in cellular adhesion and spreading processes. Previous studies implicated FAK in a wide range of human diseases, including cancer. However, it is not easy to target FAK therapeutically. In this work, the team looked at the structure of FAK and its interactions with other proteins. They found that a region in the FAK protein that contains autophosphorylation site tyrosine (Y) 397 is important for FAK activity in vivo. Additionally, they identified a direct interaction between FAK and MYO1E that increases the expression of cancer-promoting proteins. MYO1E is an actin-dependent molecular motor protein that is involved in cell adhesion and migration. This study showed that MYO1E interacts with FAK and induces FAK kinase activity and Y397 phosphorylation. Active FAK then accumulates in the cell nucleus where it up-regulates the expression of secreted cancer-promoting proteins. These secreted proteins are used by cancer cells to make scaffolds to escape the effect of the body’s anti-tumor immunity and support cancer growth and metastasis. Collectively, the results suggest that the interaction between FAK and MYO1E may contribute to cancer metastasis. Thus, inhibiting the FAK/MYO1E interaction may be a strategy to inhibit cancer progression. The study “Myosin-1E interacts with FAK proline-rich region 1 to induce fibronectin-type matrix”appears in the Proceedings of the National Academy of Science. Joel Heim from Mayo Clinic is the first author. Cusabio offers FAK, MYO1E, and rabbit polyclonal antibody.
