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. 2024 Feb 12;15:1274209. doi: 10.3389/fphar.2024.1274209

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Copyright © 2024 Hu, Wang, Shang, Lv, Chen, Gao and Chen.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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FAK domain structure. FAK consists of a central kinase domain flanked by a FERM homology domain on the N-terminal side and a C-terminal FAT domain. Both the terminal domains are separated from the kinase domain by a linker region containing proline-rich regions (PRR). Important tyrosine (Y) phosphorylation (P) sites are indicated; Y397, K454, and H58 play crucial roles in FAK activation. FAK binding partners are displayed at their interaction sites within FAK. The color signifies the function of FAK interacting proteins, which facilitate diverse activities of cancer cells by interacting with FAK (Sulzmaier et al., 2014).