Cellular redox agents contribute to a plethora of both physiological and pathophysiological processes as they can promote DNA damage as well as oxidative inactivation or activation of certain redox-active proteins.

p21Ras (Ras), Rho (i.e., Ras, Rac, Cdc42 and RhoA), and Ran1 GTPases mediate a diverse array of cellular processes. It is known that these small GTPases are redox active and aberration of their activity can lead to an increase in the amount of the biologically active form of GTPases which can promote uncontrolled cell growth.  It is also well known that Ras is the most prevalent oncoprotein found in human cancer.

In addition to these small GTPases, phosphatases and kinases also mediate various cellular signaling events.  Many phosphatases and kinases are also redox active, and perturbation of their redox signals often induces unchecked cell proliferation.

Our research efforts focus on elucidating the molecular mechanisms by which (i) redox-active small GTPases, including the proto-oncoprotein Ras, and (ii) redox-active phosphatases and kinases are regulated by cellular redox agents.


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Department of Chemistry and Biochemistry | University of Texas at Arlington