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Redox regulation of tyrosine kinase signaling: More than meet the eye.

Protein kinases are essential mediators of cellular signal transduction and are often dysregulated in disease. Among these, protein tyrosine kinase signaling has received specific interest due to their common roles in various diseases including cancer, and emerging observations indicating that this signaling pathway is susceptible to regulation by reactive oxygen species (ROS) that are also frequently implicated in disease pathology. While it is well recognized that ROS can impact on tyrosine kinase signaling by inhibiting tyrosine phosphatases, more recent studies highlight additional modes of redox-based regulation of tyrosine kinase signaling by direct redox modification of non-catalytic cysteines within tyrosine kinases or other protein components of this signaling pathway. In this review, we will present recent advancements with respect to redox-based mechanisms in regulating protein tyrosine kinase signaling, with a specific focus on recent studies demonstrating direct redox regulation of Src-family kinases and epidermal growth factor receptor kinases. Importantly, redox-based modulation of tyrosine kinases may be relevant for many other kinases and has implications for current approaches to develop pharmacological inhibitors for these proteins.