Ugo Dionne 

(co-supervision with Nicolas Bisson) PhD Student
ugo.dionne.1 [at]


I grew up in Laval where I completed high school. I then went to Montreal for my college degree. After moving to Quebec City, I did my bachelor’s degree in Biochemistry at Laval University. I did two research projects, one in Héma-Québec’s research and development department and the other in Dr. Nicolas Bisson’s laboratory at the cancer research center. Then, I started my master’s degree in Cellular and Molecular Biology at the Faculty of Medicine of Laval University under the supervision of Dr. Bisson and later started my PhD, this time in co-direction with Dr. Christian Landry.


Research interests

My main interest in research is cell signaling and more specifically the molecular mechanisms regulating the biological processes used by cells to adapt to their environment. I study protein complexes allowing the transduction of cellular signals downstream of tyrosine kinase receptors. I am interested in adaptor proteins, whose function is to recruit specific cytoplasmic effectors to activated receptors at the membrane. I am working on NCK1 and NCK2 proteins in mouse and human cell models as well as in Drosophila. I elucidated a mechanism of phospho-regulation via the tyrosine kinase receptor EphA4 and the SH3 domains of NCK1/2. My research also focuses on the large family of SH3 domains that bind proline/arginine-rich amino acid motifs. These domains are present on several types of proteins such as adapter proteins and tyrosine kinases. The overall structure of these domains is conserved through evolution. My study model for SH3 domains is yeast. I am looking to discover the amino acids of SH3 domains regulating their ability to bind their partners using PCA and genome editing using the CRISPR/Cas9 system.


Dionne U, Bourgault E*, Dubé AK*, Bradley D*, Chartier FJM*, Dandage R, Dibyachintan S, Després PC, Gish GD, Hang Pham NT, Létourneau M, Lambert JP, Doucet N, Bisson N, and Landry CR. Protein context shapes the specificity of SH3 domain-mediated interactions in vivo. Nature Communications 12, 1597 (2021)

Dionne U, Chartier F, Lopez Y, Lavoie N, Bernard DN, Banerjee SL, Otis F, Jacquet K, Tremblay MG, Jain M, Bourassa S, Gish GD, Gagné JP, Poirier GP, Laprise P, Voyer N, Landry CR, Doucet N, Bisson N. Direct phosphorylation of SRC homology 3 domains by tyrosine kinase receptors disassembles ligand-induced signaling networksMolecular cell 70(6):995-1007 (2018)

Filteau M, Diss G, Torres-Quiroz F, Dube AK, Schraffl A, Bachmann V, Gagnon-Arsenault I, Chretien AE, Steunou AL, Dionne U, Coté J, Bisson N, Stefan E & Landry CR Systematic identification of signal integration by Protein Kinase A. PNAS 112:4501-4506 (2015)