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Amber Young
University of Toledo

Subject Listing - Biology: Molecular Biology
Advisor: Dr. Brian Ashburner

Thursday, Poster Session 1, Presentation Kiosk 8 C, Health & Fitness Center

IDENTIFICATION OF CBP SITES PHOSPHORYLATED BY P38

NF-κB is a transcription factor that is involved in essential biological processes such as immune and inflammatory responses, cell proliferation, and programmed cell death. Classical NF-κB is a heterodimer of the subunits p65 and p50. The ability of NF-κB to activate transcription of genes is dependent on its interaction with transcriptional coactivators, such as the CREB-binding protein (CBP). However, the mechanisms regulating interaction between CBP and p65 is not completely understood. Therefore, the focus of my current research is to gain a better understanding of how the interaction between the p65 subunit of NF-κB and CBP is regulated. Preliminary evidence has indicated that the p38 MAP kinase is involved in regulating the p65 and CBP interaction. One potential mechanism is that p38 regulates the p65 and CBP interaction by interacting with and possibly phosphorylating CBP. Our data indicates that p38 can phosphorylate CBP at multiple sites in in vitro kinase assays; however, it is not clear if these sites are also phosphorylated in vivo. To test this, site directed mutagenesis will be used to mutate potential p38 phosphorylation sites (serine or threonine) to alanines. We will then determine if these mutant forms of CBP are still phosphorylated by p38 and will determine the effect of these mutations on the ability of CBP to function as a coactivator for NF-κB.

Advisor: Dr. Brian Ashburner, Assistant Professor, Department of Biological Sciences, University of Toledo, Toledo, OH