|Start Date / Time||October 30, 2013 at 9:00 AM|
|End Date / Time||October 30, 2013 at 10:00 AM|
|Location||512 Light Hall|
|Presenter Name||David Scoville (Stein lab)|
|Presentation Title||Identification and characterization of the novel interaction between MafA and the MLL3/4 complex|
|Status||This meeting has already occurred|
MafA and MafB, two closely related transcription factors, play critical roles in the formation of functional β-cells. My work aims to further understand the mechanisms by which MafA promotes expression of key β-cell genes. I have used a co-immunoprecipitation (co-IP) technique that utilizes “in cell” chemical cross-linking reagents to isolate MafA binding partners, and mass spectrometry (MS) to identify these proteins. I have detected as a MafA coregulator the MLL3/4 complex, which catalyzes the activating epigenetic H3K4 trimethylation (H3K4me3) mark. Experiments in a newly generated human β-cell line have shown that both MafA and MafB interact with this complex, likely through a heterodimer of MafA and MafB. I am currently working to dtermine whether MafA and the MLL3/4 complex interact in vivo in human tissue, and using mouse models containing β-cell specific deletions of MafA and NCoA6, an essential member of the MLL3/4 complex, to characterize the function of this interaction.