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Focal adhesion kinase (FAK)

Overview

Focal adhesion kinase (FAK), also known as PTK2, is a non-receptor protein tyrosine kinase that functions as a central signaling node at focal adhesions, where cells attach to the extracellular matrix through integrins. It integrates mechanical cues and adhesion-dependent signals to regulate cell migration, survival, proliferation, cytoskeletal remodeling, and mechanotransduction. Through autophosphorylation and downstream signaling, FAK helps coordinate pathways such as RhoA/ROCK, YAP/TAZ, MAPK, and other adhesion-linked cascades.

In biomedical research, FAK is widely studied as a mediator of tumor progression, invasion, therapy resistance, and tissue mechanobiology. Recent studies in the provided context also place FAK in cartilage homeostasis under cyclic tensile stress, in viscoelasticity-dependent cell adhesion and migration, and in cancer-associated signaling axes including ITGA5-FAK in liver cancer and c-met/FAK-linked oncogenic signaling in lung cancer. Because of its position at the interface of adhesion and signaling, FAK is a frequent therapeutic target in oncology and regenerative medicine.

Recent Publications Summary (latest 30 papers)

Recent studies continued to position focal adhesion kinase (FAK) as a central mediator of adhesion-dependent signaling in cancer and mechanobiology. In hepatocellular carcinoma, RPRD1A was reported to promote lenvatinib resistance by derepressing ITGA5 transcription through a c-JUN-dependent pathway, with ITGA5 then activating FAK signaling; combined lenvatinib plus the FAK inhibitor defactinib was highlighted as a rational strategy to counter resistance 42171939May. In colorectal cancer, conferone was identified as a natural compound with anti-migratory and anti-invasive activity, and it reduced FAK and phospho-FAK (Tyr397) levels while reversing epithelial-mesenchymal transition; docking analyses supported direct FAK binding and predicted inhibition of its phosphorylation 42056844Apr.

FAK was also implicated in integrin-linked mechanotransduction across engineered and physiological systems. In a breast cancer model, a structure-based peptide inhibitor targeting the talin2-β-integrin interaction suppressed proliferation, migration, invasion, and HUVEC tube formation, and it inhibited FAK phosphorylation at Y397 and Y576 while showing in vivo antitumor activity 42020994Apr. In lung cancer-focused in silico screening of Pinellia ternata phytochemicals, PTK2 (FAK) emerged among the core targets prioritized by graph-attention-guided virtual screening and multi-scale simulations, suggesting potential multi-target engagement of FAK-related pathways by bioactive compounds 42149884May.

Beyond oncology, FAK was linked to tissue mechanics and cell homeostasis. Synthetic hydrogels with programmable viscoelasticity were used to show that tissue-matching mechanical properties influence cell spreading and directional migration, with the signaling efficacy of FAK and associated YAP-related mechanosensing pathways being examined in relation to these responses 42093414May. In osteoarthritic chondrocytes, cyclic tensile stress restored anabolic/catabolic balance and cell viability through reactivation of the integrin-FAK-RhoA/ROCK2 cascade; FAK phosphorylation at Y397 increased under stress, and FAK knockdown abolished the downstream upregulation of RhoA and ROCK2, confirming FAK as an essential mediator of the protective mechanical response 41935436Apr.

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