The main focus of our lab is understanding how specific members of the protein kinase C family (PKC) function to modulate apoptosis in salivary acinar epithelial cells. We have previously shown that nuclear localization of PKCδ is both necessary and sufficient for apoptosis. In addition, our recent studies show that tyrosine phosphorylation on residues Y64 and Y155 is necessary for nuclear translocation of PKCδ and are therefore critical for pro-apoptotic signaling of PKCδ. The focus of my project to understand the mechanism by which tyrosine phosporylation on Y64 and Y155 residues regulate nuclear translocation of PKCδ.

General Interests:
Soccer, volleyball, cooking, car shows and just hanging out with friends and enjoy the many things Colorado has to offer.

Michael J. Humphries, Angela M. Ohm, Jerome Shaack, Tariq S. Adwan and Mary E. Reyland. Tyrosine Phosphorylation In The Regulatory Domain Of PKCdelta controls Nuclear Localization And Apoptosis. Oncogene 2008 May 8;27(21):3045-53.

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