NIH Proteomics Interest Group

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ProtIG is an NIH Special Interest Group (SIG) that organizes seminars and workshops in relevant areas of proteomics, including talks on separation and protein identification methods, determination of post-translational modifications, protein-protein interactions, and bioinformatics and data management. A monthly seminar series is usually held at 10 am on the Second Thursday of each month (always check the Mtgs/Seminars button on this page for these and other PROTIG announced meetings). To receive email announcements of ProtIG events, join the listserv (Join the SIG button on this page)

November ProtIG Seminar
Thursday, November 14th, 2019
10:00 am - 11:00am
Building 50, NIH Campus
Room 1227/1233 (Lobby Conference Room)
Michael Washburn, Ph.D., FRSC
Professor
Department of Pathology and Laboratory Medicine
School of Medicine, University of Kansas, Kansas City, KS

Director of Proteomics
Stowers Institute for Medical Research, Kansas City, MO


"Decoding the Diversity within Human Histone Deacetylase Protein Interaction Networks"

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.






Seminars will be webcast online at http://videocast.nih.gov and available on the
Proteomics Interest Group website http://proteome.nih.gov as an archived presentation unless otherwise noted.



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This site was updated on November 1st. Please contact Renee Olano at olanol(at)mail.nih.gov with questions or suggestions.