※ FAK family introduction

    FAKs are ubiquitously expressed non-receptor protein-tyrosine kinase. Two members have been found in human genome FAK1 and FAK2. FAKs contain a FERM domain at N-terminal followed by a protein kinase domain and a C-terminal FAT domain. FERM domain mediate the directly bind to intracellular domain of β1-integrin subunit or some membrane receptor. FERM domain is also responsible for FAK kinase catalytic activity regulation. FAT domain is responsible for FAK binding to focal adhesion complexes. FAKs keep an inactive conformation in which FERM is bound to FAK kinase domain. After release the auto-inhibitory between FERM and kinase domain, FAKs will undergo kinase activation and autophosphorylation of Y397, which will in turn produce the maximal activity. Activate FAKs will function on different substrates and lead to different effects on cell behaviors, including increased motility, integrin recycling, focal contact turnover, survival and protection from adhesion dependent apoptosis (anoikis) (1).

Reference
1. Lechertier, T. and Hodivala-Dilke, K. (2012) Focal adhesion kinase and tumour angiogenesis. J Pathol, 226, 404-412. PMID: 21984450