541 Mark Jefferson Science Complex
Ypsilanti, Michigan 48197
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.
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.