Boyko S. Atanassov
Originally from Sofia, Bulgaria
M.Sc. Sofia University, Sofia Bulgaria
Ph.D. Bulgarian Academy of Sciences/NIH
Research Interests: Functions and regulation of chromatin modifying and deubiquitinating enzymes; Epigenetics; Molecular mechanism of cancer metastasis
I was born and raised in Buffalo, NY. I attended St. John Fisher College in Rochester for my undergraduate studies. After graduating with my B.S. in Biology with a minor in Chemistry, I moved on to graduate school at the University at Buffalo where I worked in a microbiology lab focusing on studying different protein interactions with the Human Papillomavirus Helicase protein E1 in the pursuit of discovering a novel target for therapeutics. I graduated with my M.S. in Microbiology and Immunology and moved on to join the Atanassov Lab at Roswell Park as a technician in the summer of 2017 where I am working on elucidating the molecular mechanisms by which chromatin modifying enzymes impact tumor formation, growth and metastasis.
Research in my laboratory is focused on elucidating the molecular mechanisms by which chromatin modifying enzymes and the complexes they form potentiate tumor formation, growth and metastasis. Although genetic changes in cancer are well recognized, epigenetic changes that alter gene expression patterns have also been found to play a major role during development of this disease in recent years. These changes, affecting post-translational modifications of histones and DNA methylation, are mediated by various chromatin modifying enzymes. Our work has revealed that these enzymes often have functions independent of their canonical roles in transcriptional regulation that are critically important for normal cell growth, survival and response to the environment. We are particularly interested in Ubiquitin Specific Proteases (USPs) that are capable of removing ubiquitin moieties from histones, thus altering the expression patterns of target genes. In recent years many USPs have been directly linked to different stages of cancer progression. For example, USP22 is a member of an 11 gene “death-from-cancer” signature that serves as a predictor for treatment resistance, tumor aggressiveness and metastatic probability in cancer patients. Additionally, ablation of USP44 leads to spontaneous lung cancer in mice whereas its function is required for invasion of breast cancer cells in vitro. Further, in our recent studies, we identified two uncharacterized USPs, USP27X and USP51, which are remarkably similar to the cancer-associated USP22, to which their ablation severely impacts tumor growth. Thus, using a variety of biochemical and genetic approaches (e.g. tissue culture and mouse models) our lab aims to 1) define the molecular mechanisms by which USP27X, USP51, and other USPs impact tumor growth, and 2) define the in vivo functions of these USPs during normal development and carcinogenesis.
Misregulation of ubiquitin-proteasome pathways is implicated in the pathogenesis of many human diseases, particularly cancer, and proteasome inhibitors are studied as possible treatments for these diseases. Hence, inhibitors of USPs are particularly attractive for therapeutic intervention; specific inhibition of their function would operate upstream of the proteasome and possibly generate specific and less toxic antitumor therapies. Therefore, it is our long-term goal to connect the mechanistic and molecular findings in our laboratory to cancer.