Cancer Research

The cancer research group brings together an excellent mix of diverse and internationally recognized researchers to improve our understanding of cancer cell biology.  Our interdisciplinary group builds on complementary skills in order to advance research through collaboration.  We strive to understand the complexity of cancer from different aspects that include basic and translational cancer research.  Our overarching goals are to improve our understanding of the causes of cancer, identify and validate new targets for cancer therapies and apply this information to the development of new diagnostics, prognostic indicators and ultimately new therapies.  We anticipate that these discoveries will contribute to more personalized medicine and improved patient outcomes.

Dr. Deborah Anderson
Dr. Anderson is studying cell signaling downstream from receptor tyrosine kinases and the mechanisms cells use to turn off these signals.  Her lab is working to understand how the regulation of the tumor suppressor protein, PTEN, a lipid phosphatase that counteracts cell survival and proliferative signals generated by PI3K, contributes to cancer. She is also interested in studying receptor endocytosis, trafficking and degradation pathways to determine the mechanisms used by cells to switch off receptor signalling.  More recently, her lab has also been involved in studying the function of the metastasis suppressor protein CREB3L1.
Dr. Andrew Freywald
Dr. Freywald is actively working to elucidate the mechanism of ephrn-B1-induced anti-apoptotic action, which, combined with its ability to induce cell repulsion, is likely to protect T-ALL cells from immuno-elimination in patients undergoing bone marrow transplantation. His lab also examines the role of the EphB6 receptor in breast cancer and assesses EphB6 receptor potential as a novel target for breast cancer therapy to develop EphB6-activating synthetic antibodies for future utilisation in cancer treatment.
Dr. Troy Harkness
Dr. Harkness is investigating the regulation of replication-independent chromatin assembly in yeast.  His lab utilizes yeast as a model system to address how the basic unit of the chromosome (chromatin) is assembled and how this process is regulated. He is also working to understand how lifespan in eukaryotic organisms is determined and has the following aims: i) to study the role that is played by the RAS/PKA and Snf1 signaling pathways in determining APC-dependent lifespan, ii) to identify other components of the ubiquitin-dependent protein targeting cascade involved in chromatin metabolism, iii) to determine the molecular basis of APC-dependent chromatin assembly, and iv) to determine the effects on higher eukaryotic systems, such as humans and mouse, when the mitotic-specific chromatin assembly activity is compromised.
Dr. Franco Vizeacoumar
A key message from the current genomic studies is that therapeutic approaches should aim at the genetic basis rather than the tissue of origin. This knowledge and the availability of highly selective inhibitors of gene products, promises personalized medicine through a genotype-directed cancer therapy. My lab is directly involved developing such a genotype-directed cancer therapy for solid tumors by applying a basic biological concept called synthetic lethality. In effect, any genetic alteration that can cause selective-lethality with an oncogenic or a tumor suppressor mutation can be potentially translated into a therapeutic target. Our long term goal is to build a synthetic lethal network that will enable us to understand the genetic dependencies of cancer cells and define key therapeutic targets.
Dr. Yuliang Wu
The laboratory of Dr. Wu aims to understand how protein changes can lead to breast cancer and Fanconi anemia, a genetic disease that often leads to leukemia and other types of cancer. Wu and his team are looking at the Fanconi anemia group J protein, which contributes to DNA repair. He has identified changes, or mutations, in the protein in cases of breast cancer or Fanconi anemia and is conducting further research to determine the potential structural defects. This knowledge is an important step toward possible therapies that target the mutated protein.
Dr. Wei Xiao

DNA damage and genomic instability are hallmarks of cancer. Previous research in my laboratory reveals that a yeast Ubc13-Mms2 complex plays a critical role in maintaining genomic stability particularly in response to DNA damage. Ubc13 is unique among ubiquitin conjugating enzymes in that it promotes K63-linked polyubiquitination of target proteins, and this activity absolutely requires a cofactor Uev including the yeast Mms2. Mammals contain two Uev homologs: Mms2 and Uev1, and we have demonstrated that while Mms2 is involved in DNA damage response, Uev1 is required for the NF-kB mediated innate immunity, both of which are linked to cancer. It becomes more complicated in that mammals contain different Uev1 isoforms. My laboratory is interested in the molecular mechanisms of K63-linked polyubiquitination and its impact on cancer.

Dr. Erique Lukong

Research in the Dr. Lukong lab is centered on breast tumor kinase (BRK) family Kinases (BFKs) (Goel and Lukong, 2015). The BFKs includes BRK, fyn-related kinase (FRK) and Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation Sites (SRMS). BRK is overexpressed in the majority of breast carcinomas and tends to function as an oncogene, while FRK displays tumor suppressor activity in breast cancer. The cellular roles of SRMS are unknown. The Lukong lab is investigating the cellular and physiological roles, and the mechanisms of action and modes of regulation of all three kinases in breast cancer. Three recent publications from the Lukong lab have demonstrated that: 1) The enzymatic activation of BRK is important for BRK-promoted tumorigenesis (Miah et al., 2012); 2) BRK potentially promotes tumorigenesis by inducing the degradation of the tumor suppressor protein Dok1 (Miah et al., 2014); and 3) the autoregulation of SRMS (Goel et al., 2013).  The Lukong lab has also diversify into proteomic-related research to identify the interacting partners and substrates of the BFKs, crystalize the functional domains of these enzymes and to characterize their roles in signal transduction.