Biography
Overview of interests
Dr. Côté’s research focuses on the role of arginine methylation, a post-translational modification often harbored by RNA binding proteins, in the regulation of post¬transcriptional mechanisms and how these novel molecular pathways are misregulated in human pathologies such as spinal muscular atrophy (a motor neuron disease), myotonic dystrophy, Duchenne Muscular Dystrophy and cancer. His research interests are currently divided between three broad axis: (i) investigating how arginine methylation of various RNA binding proteins regulates their function under physiological and pathological settings, (ii) the normal function and role in disease of Tudor domain-containing proteins, which serve as ‘readers’ and effectors of the arginine methylation mark, and (iii) the contribution of arginine methylation to cancer.
Accomplishments / Awards
Dr. Côté’s previous work has demonstrated that the Tudor domain of SMN serves as a methyl-binding protein-protein interface involved in the assembly of various RNP complexes, including axonal RNA granules. A second major project focuses on the Tudor-containing protein TDRD3. His lab was the first report that this protein is found in cytoplasmic stress granules, and they are currently investigating the role of TDRD3 and stress granules in breast cancer. Dr. Côté also has two projects on the role of specific protein arginine methyltransferases (PRMT1v2 and PRMT7) in breast cancer. Finally, Dr. Côté’s lab entertains a number of collaborative projects within their three main research axis.
Scientific breakthroughs / impact
Dr. Côté was the recipient of the Distinguished Young Professor Award in 2008. He was also nominated for the Young Researcher Award in 2009 and currently holds the Canada Research Chair Award for RNA Metabolism. Dr. Côté ‘s work has led to the generation of key reagents (e.g. methylarginine-specific antibodies) and findings that helped pave the way for future studies investigating the role of arginine methylation in intracellular signal transduction and cancer. He has characterized alternatively spliced isoforms of the major protein arginine methyltransferase (PRMT1), that have distinct properties and, most importantly, that are overexpressed in breast cancer and contribute to metastatic potential (JBC 2007, Cell Cycle 2012). His work has also identified a novel methyl-binding protein, TDRD3, that localizes to cellular stress granules (Human Molecular Genetics 2008), a structure that is thought to contribute to the 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.
Grant support
Dr. Côté’s research is funded by the Canadian Institute for Health Research (CIHR) and a number of foundations including the Muscular Dystrophy Association (USA), Canadian Breast Cancer Foundation, Families of SMA and Association Française contre les myopathies.