The net cellular level of tyrosyl phosphorylation is regulated by the intrinsic and opposing activities of protein tyrosine kinases and protein tyrosine phosphatases (PTPs). Protein tyrosyl phosphorylation mediates numerous biological events such as mitogenesis, differentiation, cell movement, cytoskeletal function and apoptosis. Our laboratory is interested in how PTPs regulate these physiological processes. We focus our studies on the PTPs by using integrated approaches that encompass cell biology, genetics, protein biochemistry and cell imaging. To precisely define the physiological role of the PTPs, our studies are directed towards how these enzymes regulate specific cellular systems. For example, in order to explore the role of PTPs in complex differentiation and regenerative pathways, we utilize the skeletal muscle and liver systems. Elucidating how PTPs participate in regulating signal transduction will extend our understanding of the mechanisms of protein tyrosyl phosphorylation in cellular physiology.

Leite, M.F., et al. (2003). Nuclear and cytosolic calcium are regulated independently. Proc. Natl. Acad. Sci. (USA) 100(5):2975-80.

Ivins Zito, C., Kontaridis, M.I., Fornaro, M., Feng, G.S., and Bennett, A.M. (2004). SHP-2 regulates the phosphatidylinositide 3'-kinase/Akt pathway and suppresses caspase 3-mediated apoptosis. J. Cell Physiol. 199(2):227-36.