Dear Colleagues,

More than twenty-five years ago, Focal Adhesion Kinase (FAK) was described as a substrate of the oncogene product of the Rous sarcoma virus, v-Src, and as a protein, highly phosphorylated upon clustering of integrins at focal adhesions. Consequently, FAK was shown to be primarily implicated in the regulation of signals initiated at sites of integrin-mediated cell adhesion, as well as signals triggered upon growth factor receptors activation.

Subsequent studies revealed that FAK plays fundamental roles in cell survival, growth, motility, and invasion. Thus, FAK is involved in many aspects of the metastatic process, as well as overexpression, hyperphosphorylation, and/or elevated activity of FAK, have been reported in a variety of human cancers, including sarcomas and carcinomas associated with tumor growth, neoangiogenesis and metastatic dissemination. In addition to its localization at focal adhesions, FAK was recently found in unexpected places, including endosomes and adherent junctions. The new role for nuclear FAK has also been recognized and new insights were made on the mechanism of FAK dimerization and its role in FAK activity.

The development of FAK antagonists, as anti-cancer therapy, led to several small inhibitors of FAK kinase function that are currently undergoing clinical trials. In addition to its kinase function, FAK possesses scaffolding functions that are highly relevant in cancer signalling. New and recent investigations also showed that FAK antagonists may display therapeutic benefits in cancer patients by acting on the immune system, triggering T-cells-mediated immune response. FAK antagonists may also be used to reduce cancer resistance, notably when associated with BRAF inhibitors in melanoma patients.

This Special Issue will highlight the current state-of-the-art in FAK biology and future prospects for improving therapies.

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