Focal Adhesion Kinase
Focal adhesion kinase (FAK), a non-receptor tyrosine kinase, is the first intracellular step in the signal transduction cascade initiated by the attachment of an integrin to the extracellular matrix at points known as focal adhesions. Therefore, FAK plays a key role in cellular migration and motility.
FAK has 3 functional domains: a focal adhesion targeting domain (FAT), a catalytic domain and a FERM domain, which mediates interactions with the cytoplasmic domains of integrins and growth factor receptors. FAK has multiple phosphorylation sites that are required for binding to adaptor proteins containing SH2 domains (e.g. Src and SH3 domains (e.g. CAS, GRAF)). Key amongst these phosphorylation sites is Tyr397, which is important for the interaction of FAK with downstream signaling molecules such as PI 3-K, PLCγ and Rho kinase.
Overexpression of FAK has been associated with several types of cancer.View all products for Focal Adhesion Kinase »
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Literature for Focal Adhesion Kinase
A collection of over 750 products for cancer research, the guide includes research tools for the study of:
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