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Decoding the Diversity within Human Histone Deacetylase Protein Interaction Networks

Air date: Thursday, November 14, 2019, 10:00:00 AM
Time displayed is Eastern Time, Washington DC Local
Description: Proteomics Interest Group

The efficacy of HDAC inhibitors (HDACis) as chemotherapeutic agents is a topic of many ongoing clinical studies. Despite the current existence of 4 FDA-approved HDACis, the molecular mechanisms that mediate their effectiveness and off-target effects are poorly defined. Among HDAC complexes that are targeted by HDACis, Sin3 complexes have important roles in the regulation of transcriptional activity and may mediate many the effects of these compounds. Sin3 complexes are named for the scaffolding protein of the complexes and have forms conserved from yeast to humans. However, the acquisition of additional Sin3 complex components by humans that are not present within the well characterized yeast forms of the complex contributes to our poor understanding of the functional attributes of human Sin3 complexes. Using quantitative proteomics, we characterize the human Sin3 interaction network and provide definition to the human Sin3 complex population. We show that the interaction networks of the two human Sin3 protein paralogs, SIN3A and SIN3B, only partially overlap and that the identity of the Sin3 protein paralog within a complex influences complex composition. Through the comparison of SIN3A and SIN3B protein features, we reveal shared and divergent attributes that have functional consequences. Our results provide definition to the heterogeneous population of Sin3 complexes and highlight the need for future studies to assess the biological consequences of diversity within populations of HDAC complexes.

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Author: Michael Washburn, Ph.D., Director of Proteomics Center, Professor, Department of Pathology & Laboratory Medicine, University of Kansas Medical Center
Runtime: 1 hour