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The Cheminar: Mary Kay H. Pflum, Ph.D.

Tuesday, April 30, 2024
11:00 a.m. - 12:00 p.m.

Add to Calendar 2024-04-30 11:00:00 2024-04-30 12:00:00 The Cheminar: Mary Kay H. Pflum, Ph.D. Tuesday, Apr. 30 | 11 a.m. - 12 p.m.Classroom Building 170 Histone Deacetylase Enzymes: Substrate identification to Discover New BiologyHistone deacetylase (HDAC) enzymes are key players in cancer progression and have emerged recently as targets for anti-cancer drugs. In fact, four drugs are currently used clinically to treat leukemia and lymphoma. While HDAC activity has been intensely studied, A significant challenge in the HDAC research field lies in the fact that HDAC substrate selectivities are poorly understood. HDAC enzymes catalyze the deacetylation of acetyllysine residues on protein substrates. The oldest and most well studied protein substrates are histone proteins. In fact, studies of histone deacetylation by HDAC proteins have been key to development of HDAC inhibitor anti-cancer drugs. However, recently many, many acetylated proteins have been identified in cells, which strongly suggests that HDAC enzymes deacetylate substrates beyond histones. Unfortunately, few approaches are available to identify the substrates of HDAC proteins. To facilitate identification of HDAC substrates and reveal novel biology associated with HDAC proteins, we have developed “substrate trapping mutants”. Using substrate trapping mutants, we identified several new substrates of HDAC proteins. These new substrates have revealed novels roles of HDAC proteins is cell division and gene regulation, which are unregulated incancer. Through inhibitor substrate identification, this substrate identification project in the Pflum lab will deepen our understanding of basic biological mechanisms, as well as cancer onset and progression.About the SpeakerDr. Pflum received a B.A. degree from Carleton College working with Jerry Mohrig in physical organic chemistry. In Ph.D. training at Yale University with Alanna Schepartz, she worked on several bioorganic projects focusing on phosphoproteins and transcription factors. In an NIH post-doctoral position at Harvard University with Stuart Schreiber, she worked on chemical biology and cell biology projects focusing on histone deacetylase proteins. Dr. Pflum joined the faculty at Wayne State University in 2001 with a research program at the interface of Chemistry and Biology focusing on two cancer-related proteins – kinase and histone deacetylase enzymes. The multi-disciplinary research in her laboratory combined the fields of organic synthesis, biochemistry, enzymology, molecular biology, analytical chemistry, and cell biology. 3601 Pacific Ave, Stockton, CA 95211, USA College of the Pacific College of the Pacific America/Los_Angeles public

Tuesday, Apr. 30 | 11 a.m. - 12 p.m.
Classroom Building 170

Histone Deacetylase Enzymes: Substrate identification to Discover New Biology

Histone deacetylase (HDAC) enzymes are key players in cancer progression and have emerged recently as targets for anti-cancer drugs. In fact, four drugs are currently used clinically to treat leukemia and lymphoma. While HDAC activity has been intensely studied, A significant challenge in the HDAC research field lies in the fact that HDAC substrate selectivities are poorly understood. HDAC enzymes catalyze the deacetylation of acetyllysine residues on protein substrates. The oldest and most well studied protein substrates are histone proteins. In fact, studies of histone deacetylation by HDAC proteins have been key to development of HDAC inhibitor anti-cancer drugs. However, recently many, many acetylated proteins have been identified in cells, which strongly suggests that HDAC enzymes deacetylate substrates beyond histones. Unfortunately, few approaches are available to identify the substrates of HDAC proteins. To facilitate identification of HDAC substrates and reveal novel biology associated with HDAC proteins, we have developed “substrate trapping mutants”. Using substrate trapping mutants, we identified several new substrates of HDAC proteins. These new substrates have revealed novels roles of HDAC proteins is cell division and gene regulation, which are unregulated in
cancer. Through inhibitor substrate identification, this substrate identification project in the Pflum lab will deepen our understanding of basic biological mechanisms, as well as cancer onset and progression.

About the Speaker

Dr. Pflum received a B.A. degree from Carleton College working with Jerry Mohrig in physical organic chemistry. In Ph.D. training at Yale University with Alanna Schepartz, she worked on several bioorganic projects focusing on phosphoproteins and transcription factors. In an NIH post-doctoral position at Harvard University with Stuart Schreiber, she worked on chemical biology and cell biology projects focusing on histone deacetylase proteins. Dr. Pflum joined the faculty at Wayne State University in 2001 with a research program at the interface of Chemistry and Biology focusing on two cancer-related proteins – kinase and histone deacetylase enzymes. The multi-disciplinary research in her laboratory combined the fields of organic synthesis, biochemistry, enzymology, molecular biology, analytical chemistry, and cell biology.