Focal adhesion kinase (FAK) has an astonishing number of ligands and functions, which enable it to contribute to embryonic development and human health. FAK can promote different effects in similar cellular environments or similar effects in different cellular environments. Recent advances in structural and cellular analysis of FAK are starting to reveal the interrelationships between the conformations, localizations, interactions, and functions of FAK. This review focuses on our emerging understanding of how the structural framework of FAK mechanistically allows it to integrate manifold stimuli into environment-specific functions.
Bibliographical noteFunding Information:
I apologize to all colleagues whose work could not be explicitly mentioned due to restrictions in space and number of references. I thank J.-A. Girault, D. Arsenieva, Z. Lu and J.E. Ladbury for critical reading of this manuscript and K. Muller for editorial assistance. This research is supported in part by the National Institutes of Health through MD Anderson's Cancer Center Support Grant ( CA016672 ). This research was supported by the University Cancer Foundation via the Institutional Research Grant program at the University of Texas MD Anderson Cancer Center.
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology