Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, Western General Hospital, Crewe Road South, Edinburgh EH4 2XR, UK.
Nat Rev Mol Cell Biol. 2010 Nov;11(11):802-14. doi: 10.1038/nrm2996.
Focal adhesion kinase (FAK) is a scaffold and tyrosine kinase protein that binds to itself and cellular partners through its four-point-one, ezrin, radixin, moesin (FERM) domain. Recent structural work reveals that regulatory protein partners convert auto-inhibited FAK into its active state by binding to its FERM domain. Further, the identity of FAK FERM domain-interacting proteins yields clues as to how FAK coordinates diverse cellular responses, including cell adhesion, polarization, migration, survival and death, and suggests that FERM domains might mediate information transfer between the cell cortex and nucleus. Importantly, the FAK FERM domain might act as a paradigm for the actions of other FERM domain-containing proteins.
黏着斑激酶（FAK）是一种支架和酪氨酸激酶蛋白，通过其四肽重复结构域（FERM）与自身和细胞伙伴结合。最近的结构研究表明，调节蛋白伴侣通过与 FAK 的 FERM 结构域结合将自身抑制的 FAK 转化为其活性状态。此外，FAK FERM 结构域相互作用蛋白的鉴定为 FAK 如何协调多种细胞反应提供了线索，包括细胞黏附、极化、迁移、存活和死亡，并表明 FERM 结构域可能介导细胞皮层和细胞核之间的信息传递。重要的是，FAK FERM 结构域可能是其他 FERM 结构域蛋白的作用模式。
