Brittany Albaugh
Education
Biochemistry
- BS, Grand Valley State University
- Ph.D., University of Wisconsin-Madison
- Postdoc, University of Wisconsin Madison
Interests and Expertise
My research interest is to understand the molecular mechanisms underlying cancer development and the role of epigenetics in cancer. Within 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 and Presentations
Liu W, Miner R, Albaugh BN , Ananiev G , Wildman S, Denu JM. Discovery and Mechanism of Small Molecule Inhibitors Selective for the Chromatin binding domain of Oncogenic UHRF1. ACS Biochemistry. Accepted. 2022.
Albaugh BN, Denu JM. Catalysis by Protein Acetyltransferase Gcn5. Biochimica at Biophysica Acta (BBA)- Gene Regulatory Mechanisms. 2021. 1864:2.
Ginnard SM, Winkler AE, Fritz CM, Bluhm T, Kemmer R, Gilliam M, Butkevich N, Abdrabbo S, Bricker K, Feiler J, Miller I, Zoerman J, El-Mohri Z, Khuansanguan P, Basch M, Petzold T, Kostoff M, Konopka S, Kociba B, Gillis T, Heyl DL, Trievel RC, Albaugh BN, Molecular investigation of the TTD and PHD histone binding domains of the epigenetic regulator UHRF2 Proteins: Structure, Function and Bioinformatics. 2022; 90:835-847. https://onlinelibrary.wiley.com/doi/10.1002/prot.26278.
- Meyer K, Albaugh BN, 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.