Title:
Associate Professor

Institute: 
University of Ottawa

Department: 
Cellular and Molecular Medicine

Province:
Ontario

Training:
Senior Postdoctoral Fellow, Lady Davis Institute, McGill University, Montreal, Quebec
Postdoctoral Fellow, Washington University in St. Louis, St. Louis, Missouri, USA
PhD, Université de Sherbrooke, Sherbrooke, Quebec
BSc, Université de Sherbrooke, Sherbrooke, Quebec

Research interests:
Arginine Methylation
Post-transcriptional regulatory mechanisms
Molecular and Cellular basis of Cancer

Recognitions:
2010-15 Canada Research Chair (Tier 2) in RNA Metabolism
2008 Faculty of Medicine “Young Professor Award”
2006-11 Early Researcher Award from the Ontario Ministry of Research and Innovation
2005-10 Canada Research Chair (Tier 2) in RNA Metabolism
2005 CIHR New Investigator Award (Declined)
2001 Terry Fox Research Fellowship from the National Cancer Institute of Canada (NCIC)
2001 Postdoctoral Fellowship from the Canadian Institute of Health Research (CIHR)
1998 Postdoctoral Fellowship from the Natural Sciences and Engineering Research Council

Career highlights:
My work as a postdoctoral fellow at McGill led to the generation of key reagents (e.g. methylarginine-specific antibodies) and findings (e.g. characterization of a protein module that specifically recognize methylated arginines in proteins) helped pave the way for future studies investigating the role of arginine methylation in intracellular signal transduction and cancer. 
After starting my own research group, we have characterized alternatively spliced isoforms of the major Protein Arginine Methyltransferase (PRMT1), that have distinct properties and, most importantly, that are overexpressed in breast cancer. 
Our work has also identified a novel methyl-binding protein, TDRD3, that localizes to cellular stress granules, a structure that is thought to contribute to survival of cancer cells at the core of solid tumours, suggesting that arginine methylation may regulate the assembly and/or function of these cellular structures.

Research Projects

Project title:
The Role of PRMT1 Alternatively Spliced Isoform v2 in Breast Cancer Pathogenesis

Funding period: 
2011-2013

Program:
Operating Grant (Basic Research)

Summary:
My laboratory studies a protein modification, arginine methylation, that can change and regulate the function of proteins. We have discovered that the molecules responsible for this modification, the PRMTs, are found at abnormally high levels in breast cancer. Hence, we wish to test if defects in the cellular pathways that PRMTs normally control or regulate are contributing to the developpment and progression of breast cancer.
Specifically, we have characterized the expression of 3 different PRMTs as new biomarkers for breast cancer. We have then focused our efforts on one of these PRMTs and found that it's major role in breast cancer cells is to help them grow uncontrollably and prevent them from activating mechanisms that would lead to their elimination by the body. Since this specific form of PRMT is almost exclusively found in cancer cells and not in normal breast cells, we now propose to assess if it may be used as a potential new target to selectively eliminate tumour cells (or at least stop their growth) without affecting the adjacent normal tissues.

CRS publications:

Chen, Y.C., Milliman, E.J., Goulet, I., Côté, J., Jackson, C.A., Vollbracht, J.A. and Yu, M.C. (2010) Protein arginine methylation facilitates co-transcriptional recruitment of pre-mRNA splicing factors. Molecular and Cellular Biology, 30(21):5245-56. (partial)

Zhao, T.T., Cloutier, M., Lewis, S.M., Graber, T.E., Jordan, L, Goulet, I., Côté, J. and Holcik, M. (2009) hnRNP A1 regulates NFkB signaling via destabilization of cIAP1 mRNA. Cell Death and Differentiation, 16(2):244-52. (partial)

Goulet, I., Boisvenue, S., Mokas, S., Mazroui, R. and Côté, J. (2008) TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules. Human Molecular Genetics, 17(19):3055-74. (partial)

Goulet, I., Gauvin, G., Boisvenue, S. and Côté, J. (2007) Alternative splicing yields protein arginine methyltransferase 1 isoforms with distinct activity, substrate specificity and subcellular localization. Journal of Biological Chemistry; 282(45):33009-21. (Project fully supported by CRS funds)

Past CRS projects:

2008 The Contribution of Specific Protein Arginine Methyltransferases and their substrates to Breast Cancer Tumorigenesis

2004 The role of arginine methylation by protein arginine-N-methyltransferase I isoforms in breast cancer