The major interest in our laboratory is to understand the role of protein acetylation and deacetylation in various signal transduction pathways. We have focused our effort on dissecting the function of a family of acetyltransferase and deacetylase.
On the acetyltransferase front, we concentrate our effort on p300 and CBP family members. Inactivation of CBP/p300 by the potent viral oncoprotein E1A or by genetic mutation leads to oncogenic transformation, suggesting a critical role of CBP/p300 in cancer formation. Our laboratory is interested in dissecting out the molecular mechanism by which CBP/p300 regulate oncogenesis, and how CBP/p300-mediated acetylation events may contribute to this process.
Our current emphasis is on the study of CBP/300-mediated acetylation of p53 tumor suppressor. We are studying the impact of acetylation and deacetylation on the activities of p53. We have shown that the opposing forces of p300 and p53 deacetylase regulate p53 acetylation level and its activity.
We are also characterizing several novel deacetylases that have different biological properties. The analysis of these novel deacetylases will further elucidate the function of protein acetylation.
On the genetic front, we used genetic mating and phenotypic analysis using knockout mouse and Drosophila to determine the function of CBP/p300 in growth and differentiation control.
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