1H, 15N and 13C assignments of the targeting (FAT) domain of focal adhesion kinase.
1H, 15N and 13C assignments of the targeting (FAT) domain of focal adhesion kinase.
复制标题
粘着斑激酶靶向 (FAT) 结构域的 1H、15N 和 13C 分配。
DOI：
10.1023/a:1015371216689
复制
发表时间：
2002
影响因子：
2.7
通讯作者：
Zheng,Jie
中科院分区：
文献类型：
--
作者：
Liu,Gaohua;Guibao,CristinaD;Zheng,Jie
Focal adhesion kinase (FAK) is a nonreceptor kinase that can be activated by integrin signaling. Since the discovery of FAK in the early 1990s, this protein and its related signaling pathways have been studied in some detail (Cary and Guan, 1999; Schlaepfer et al., 1999). It is now clear that FAK plays an important role in relaying the signals that are generated by the attachment of cells to the extracell matrix (ECM), and which are transmitted through integrins to cytoplasmic and nuclear targets. In this way, FAK regulates cellular processes such as migration, survival, and proliferation (Parsons et al., 2000). The C-terminal part of FAK is rich with protein-protein interaction sites. In certain cells, this part of FAK is autonomously expressed (Hildebrand et al., 1993) and termed FAK-related non kinase (FRNK). FRNK contains a C-terminal focal adhesion targeting (FAT) domain and several prolinerich regions that serve as docking sites for many SH3-containing proteins. It acts as an endogenous inhibitor of FAK signals (Taylor et al., 2001). Upon activation, FAK colocalizes at focal adhesions (Cary and Guan, 1999; Schlaepfer et al., 1999), and mutation studies have shown that the FAT domain is responsible for this localization.Much is known about the role of FAK in integrin signaling. However, the mechanism by which activated FAK localizes to focal adhesions remains unclear. Although extensive genetic and biochemical studies of this area have been performed (Schlaepfer et al., 1999), the lack of detailed structural information about FAK and the proteins with which it interacts has
