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Focal adhesion kinase regulation by oxidative stress in different cell types
M H Ben Mahdi1, V Andrieu, C Pasquier
1INSERM U 479, Paris, France.
Abstract:
Focal adhesion kinase (FAK) is a tyrosine kinase ubiquitously expressed in cells. It was initially shown to be the initiator of focal adhesion formation in adherent cells, after its binding to integrins which induce its autophosphorylation. However, it can be also activated by a great variety of other stimuli able to act on different intracellular signaling. Reactive oxygen species (ROS), which have been shown to act as external or internal cell stimuli, induce tyrosine phosphorylation of FAK. Its autophosphorylation is followed by a submembranous localization which is crucial for many of the biological roles of FAK, including cell spreading, cell migration, cell proliferation, and prevention of apoptosis. It plays an important role in development of tumor cells, its regulation could be thus a way of impairing cell proliferation in cancer. We describe in this review the structure, activity, and functions of FAK in different cells and how ROS are able, like other stimuli, to induce its phosphorylation and modification of cell morphology and structure. The link between ROS and FAK activation could explain the role of ROS in mediating cell proliferation, cell migration, or apoptosis.
Insights
Reactive oxygen species (ROS) activate focal adhesion kinase (FAK), a key regulator of cell behavior. This activation influences cell migration, proliferation, and apoptosis, offering potential cancer therapy targets.
Area of Science:
- Cell Biology
- Biochemistry
- Cancer Research
Background:
- Focal adhesion kinase (FAK) is a ubiquitous tyrosine kinase involved in cell adhesion and signaling.
- FAK initiates focal adhesion formation upon integrin binding and subsequent autophosphorylation.
- FAK activity is modulated by diverse intracellular and extracellular stimuli.
Purpose of the Study:
- To review the structure, activity, and functions of FAK in various cell types.
- To elucidate the role of reactive oxygen species (ROS) in FAK phosphorylation and activation.
- To explore the implications of ROS-mediated FAK activation in cellular processes and cancer.
Main Methods:
- Literature review synthesizing existing research on FAK and ROS.
- Analysis of signaling pathways linking ROS to FAK phosphorylation.
- Examination of FAK's role in cell morphology, migration, proliferation, and apoptosis.
Main Results:
- ROS act as stimuli that induce tyrosine phosphorylation of FAK.
- FAK autophosphorylation leads to submembranous localization, critical for cell functions.
- ROS-induced FAK activation is linked to altered cell spreading, migration, proliferation, and apoptosis.
Conclusions:
- FAK plays a significant role in tumor cell development and progression.
- ROS-induced FAK phosphorylation is a key mechanism influencing cell behavior.
- Targeting ROS-mediated FAK activation presents a potential strategy for cancer therapy.