Research Interests

Reversible protein phosphorylation is indispensable for regulation of virtually all cellular functions. In particular, a variety of protein kinases and phosphatases are involved in intracellular signal transduction in any eukaryotic cell. Another ubiquitous signaling mechanism relies on heterotrimeric G proteins and a multitude of receptors coupled to them. While regulation of protein kinases via activation of G proteins is well documented, much less is known about G protein-dependent regulation of protein phosphatases. Recent evidence has implicated heterotrimeric G proteins G12 and G13 as direct interactors and activators of a protein Ser/Thr phosphatase PP5. On the other hand, PP5 has been found to interact with and deactivate the apoptosis signal regulating kinase 1 (ASK1), which transduces a variety of stress stimuli leading to apoptosis (programmed cell death). Moreover, findings from our laboratory indicate that G12 and G13 are able to stimulate ASK1, suggesting a complex interplay between these proteins in regulation of stress-induced apoptosis.

My current research focuses on understanding the functional interrelationships between G12/G13, PP5 and ASK1, as well as a search for additional mechanisms of their regulation. This work would lead to a better understanding of the molecular mechanisms that determine susceptibility of the cells to the stress-induced apoptosis.