Focal adhesion kinase (FAK) (FAK)

Focal adhesion kinase (FAK), also known as protein tyrosine kinase 2 (PTK2), is a non-receptor tyrosine kinase that serves as a critical integrator of signals from the extracellular matrix (ECM) and growth factor receptors [6, 10]. It is frequently overexpressed in advanced solid tumors, where it mediates essential crosstalk between cancer cells and the surrounding stroma, particularly cancer-associated fibroblasts (CAFs) [6, 9]. FAK signaling is vital for the maintenance and self-renewal of cancer stem cells (CSCs) and the promotion of the epithelial-mesenchymal transition (EMT), which facilitates metastasis and therapeutic resistance [6, 11]. By regulating the physical and chemical properties of the tumor microenvironment, FAK promotes a pro-tumorigenic niche and helps tumors evade immune surveillance [9, 12]. Therapeutic strategies targeting FAK involve small-molecule inhibitors, such as defactinib (VS-6063), which are being evaluated in clinical trials to sensitize tumors to chemotherapy and immunotherapy [6, 11]. The phrase "undisclosed signaling pathway in cancer stem cells involved in tumor–stromal interactions" was historically used as a placeholder for FAK in early drug development pipelines, such as those from Verastem Oncology, reflecting its multifaceted role in tumor biology [4, 6].

Other names

PTK2Protein tyrosine kinase 2Focal adhesion kinase 1FADK1pp125FAK

Small-molecule inhibition of the FAK kinase domain, preventing autophosphorylation and downstream signaling