Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Focal Adhesion Kinase

  • Jörg Haier
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_2228-2

Definition

The non-receptor protein tyrosine kinase focal adhesion kinase (FAK) was originally isolated as a tyrosine-phosphorylated 125-kDa protein in v-Src-transformed chicken embryo fibroblasts (3, 6, 7). FAK is a signal transducer of integrins and their interactions with certain soluble growth factors and chemokines (4). This kinase is involved in cellular processes like cell adhesion and spreading, migration, proliferation, and cell survival.

Characteristics

The focal adhesion kinase (FAK) consists of a central kinase domain, of a large N-terminal FERM domain (protein 4.1, ezrin, radixin, and moesin homology), and of a large C-terminal FAT domain (focal adhesion targeting domain). Additionally, it comprises three proline-rich regions. The FERM domain mediates interactions of FAK with growth factor receptors EGFR (epidermal growth factor receptor) and PDGF (platelet-derived growth factor receptor), which are often overexpressed in tumors and promote cell motility and invasion. The...

Keywords

FERM FAT and kinase domains FAK phosphorylation and regulation Signaling pathways in cancer Focal adhesions 
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References

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See Also

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  21. (2012) Phosphorylation. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 2870. doi:10.1007/978-3-642-16483-5_4544Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Comprehensive Cancer Center MünsterUniversity Hospital MünsterMünsterGermany