Mentor: Dr. Daiqing Liao
College of Medicine
"I have always been fascinated by research and when I came to UF, the opportunity to start doing research for myself was something that I couldn't pass up. I was lucky enough to find a project that I am passionate about and that I believe could truly make a difference in our understanding of cancer cell biology and treatment options in the future."
Biology and Spanish
- Biochemistry/Molecular Biology
- Cancer Cell Biology
- Cell Cycle Regulatory Pathways
Hobbies and Interests
Cellular Factors that Determine the Interactions of Daxx and p53
Daxx is a multi-functional protein that interacts with many cellular proteins. The Liao laboratory discovered specific interactions between Daxx and tumor suppressor p53. Later studies in the Liao laboratory identified two sequence motifs called SUMO-interacting motifs (SIMs) in Daxx that interact specifically with small ubiquitin-like modifiers (SUMOs). The main focus of my research is to understand what determines the Daxx-p53 interactions in cells. We found recently that SIMs in Daxx are critical for binding SUMO-modified p53. My experiments also show that DNA damage induced by chemotherapeutic drug etoposide markedly enhances the accumulation of Daxx and SUMO-modified p53 in a nuclear substructure called PML-body. One folded domain of Daxx has been shown recently to bind histone variant H3.3. It is thought that through this interaction, Daxx acts as a specific chaperone for H3.3 to prevent promiscuous interactions of this histone in cells before being integrated into chromatins. I will examine the interactions of p53 and various Daxx constructs with the deletions of various domains to determine whether other domains in Daxx in addition to SIMs are also important for Daxx-p53 interaction under both normal conditions and after DNA damage. I will also test whether H3.3 overexpression would impact Daxx-p53 interaction. My research will identify critical regions of Daxx for interaction with the p53 as well as the influence of Daxx’s histone chaperone function on its interaction with p53.