Eastern Michigan University
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Brittany Albaugh, Ph.D.

Assistant Professor

Dr. Brittany Albaugh 501D Mark Jefferson Science Complex

734.487.6992

balbaug1@emich.edu

Education

B.S., Grand Valley State University
Ph.D., University of Wisconsin-Madison
Postdoc, University of Wisconsin Madison
Biochemistry

Interests and Expertise

My research interest is to understand the molecular mechanisms underlying cancer development and the role of epigenetics in cancer

ChromatinWithin the nucleus of eukaryotic cells, DNA wraps around histone proteins to form nucleosomes, which allows for the compaction of chromatin. Histones and DNA can undergo covalent modification, which include acetylation, methylation and phosphorylation. These modifications are a form of epigenetic regulation and are binding partners for histone “reader” proteins that specifically recognize and interact with the modification, to then either turn on or off a nearby gene.

We study a family of histone reader proteins called UHRF1 and UHRF2 which have interesting roles in cancer development. UHRF1 and UHRF2 bind modified histones in order to downregulate gene expression and control DNA methylation. The goal of our lab is to elucidate the molecular and structural mechanisms by which UHRF1 and UHRF2 interact with modified histone proteins. By learning more about these molecular interactions, we may eventually be able to develop drugs that can specifically target UHRF1 and UHRF2 for the treatment of cancer.

Publications

  • Albaugh B.N, Meyer K, Schoenike B, Roopra A.S. REST regulates the PRC2 complex to enhance cancer aggression in Triple Negative Breast Cancer. 2015. Manuscript in preparation.
  • Meyer K, Albaugh B.N, Schoenike B, Roopra A.S. Igf1r/irs1 signaling confers pathogenic activity on breast tumor cells upon Rest loss. Molecular Cell Biology. 2015. Article in press.
  • Albaugh BN, Wagner EK, Denu JM. High-throughput strategy to identify inhibitors of histone-binding domains. Methods in enzymology. 2012;512:161-185
  • Albaugh BN, Arnold KM, Lee S, Denu JM. Autoacetylation of the histone acetyltransferase rtt109. The Journal of biological chemistry. 2011;286:24694-24701
  • Albaugh BN, Arnold KM, Denu JM. Kat(ching) metabolism by the tail: Insight into the links between lysine acetyltransferases and metabolism. Chembiochem : a European journal of chemical biology. 2011;12:290-298
  • Kolonko EM, Albaugh BN, Lindner SE, Chen Y, Satyshur KA, Arnold KM, Kaufman PD, Keck JL, Denu JM. Catalytic activation of histone acetyltransferase rtt109 by a histone chaperone. Proceedings of the National Academy of Sciences of the United States of America. 2010;107:20275-20280
  • Albaugh BN, Kolonko EM, Denu JM. Kinetic mechanism of the rtt109-vps75 histone acetyltransferase-chaperone complex. Biochemistry. 2010;49:6375-6385
  • Hallows WC, Albaugh BN, Denu JM. Where in the cell is sirt3?--functional localization of an nad+-dependent protein deacetylase. The Biochemical journal. 2008;411:e11-13
  • Berndsen CE, Albaugh BN, Tan S, Denu JM. Catalytic mechanism of a myst family histone acetyltransferase. Biochemistry. 2007;46:623-629
  • Wallar BJ, Stropich BN (maiden name), Schoenherr JA, Holman HA, Kitchen SM, Alberts AS. The basic region of the diaphanous-autoregulatory domain (dad) is required for autoregulatory interactions with the diaphanous-related form in inhibitory domain. The Journal of biological chemistry. 2006;281:4300-4307.

 

Website


Current Federal Funding Support

NSF-RUI Grant Award #1715892

The Department of Chemistry is part of the College of Arts & Sciences, 214 Pray-Harrold