Omid Haji-Ghassemi, PhD
PhD - BiochemistryUniversity of Victoria 2015
BSc Honours - Microbiology
University of Victoria 2009
Areas of Research
Structural Biology of Protein Kinases
Protein Kinases are enzymes that catalyze the transfer of a chemical tag to various amino acids of target proteins or substrates. This chemical tag is known as “phosphoryl group”, and the process is thereby termed "phosphorylation". Phosphorylation of a target protein can fine tune its activity or in some cases act as a molecular switch, turning the targeted protein on or off. This process is involved in every facet of human physiological activity from memory formation to the beating of our hearts. Aberrant phosphorylation events have been proposed to underlie many human diseases, including Alzheimer’s disease, cancer, and many different heart conditions. We are interested in how these protein kinases regulate the function of various proteins in neuronal, muscular and neuromuscular junctions; from ion channels to adapter proteins. To study these systems, we use structure-function approaches. Primarily, the lab uses X-ray crystallography and single particle cryo-electron microscopy combined with biophysical and biochemical assays to study the function of the protein kinases. Our over-arching goal is to uncover the molecular mechanisms of under-studied kinases and develop novel therapeutic tools that alter their activities. High-resolution structures often provide clues for how to alter their functions using site-directed mutagenesis or reveal novel pockets that can be used for structure-based drug design. Together these approaches contribute to our understanding of these fascinating enzymes, while at the same time provide new therapeutic strategies and for creating novel treatments against common human afflictions.
Protein Kinases are enzymes that catalyze the transfer of a chemical tag to various amino acids of target proteins or substrates. This chemical tag is known as “phosphoryl group”, and the process is thereby termed "phosphorylation". Phosphorylation of a target protein can fine tune its activity or in some cases act as a molecular switch, turning the targeted protein on or off. This process is involved in every facet of human physiological activity from memory formation to the beating of our hearts. Aberrant phosphorylation events have been proposed to underlie many human diseases, including Alzheimer’s disease, cancer, and many different heart conditions. We are interested in how these protein kinases regulate the function of various proteins in neuronal, muscular and neuromuscular junctions; from ion channels to adapter proteins. To study these systems, we use structure-function approaches. Primarily, the lab uses X-ray crystallography and single particle cryo-electron microscopy combined with biophysical and biochemical assays to study the function of the protein kinases. Our over-arching goal is to uncover the molecular mechanisms of under-studied kinases and develop novel therapeutic tools that alter their activities. High-resolution structures often provide clues for how to alter their functions using site-directed mutagenesis or reveal novel pockets that can be used for structure-based drug design. Together these approaches contribute to our understanding of these fascinating enzymes, while at the same time provide new therapeutic strategies and for creating novel treatments against common human afflictions.
Supervising degrees
Biological Sciences - Masters: Seeking Students
Biological Sciences - Doctoral: Seeking Students
More information
Working with this supervisor
The ideal candidate would be a curious and highly motivated undergraduate or master student with degree completed in Biochemistry, Molecular Biology, Chemistry or Physical Chemistry or other closely related disciplines. Prior experience with molecular biology techniques, protein biochemistry/structural biology is desired, but not critical. Though applicants with prior research experience are preferred.
Selected publications (*denotes equal contribution)
- Woll, K. A*., Haji-Ghassemi, O*., and Van Petegem F. (2021) Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM. Nat Commun 12: 1–13. [co-first author].
- Ma, R*., Haji-Ghassemi, O*., Ma, D*., Jiang, H*., Lin, L., Yao, Li., Samurkas, A., Li, Y., Wang, Y., Cao, P., Wu, S., Zhang, Y., Murayama, T., Moussian, B., Van Petegem, F., and Yuchi, Z. (2020) Structural Basis for Diamide Modulation of Ryanodine Receptor. Nat Chem Biol 16: 1246–1254. [co-first author].
- Haji-Ghassemi, O., Yuchi Z., and Van Petegem F. (2019) The cardiac ryanodine receptor phosphorylation hotspot embraces PKA in a phosphorylation-dependent manner. Mol Cell 75, 39–52.
- Roston TM*., Haji-Ghassemi O*., LaPage M.J., Batra A.S., Bar-Cohen Y., Anderson C., Lau Y.R., Maginot K., Gebauer R.A., Etheridge S.P., Potts J.E., Van Petegem F., Sanatani S. (2018) Catecholaminergic polymorphic ventricular tachycardia patients with multiple genetic variants in the PACES CPVT Registry. PLoS One 13: e0205925. [co-first author].
- Haji-Ghassemi O, Gagnon SML, Muller-Loennies S, Evans SV. (2017) Polyspecificity of anti-lipid an antibody and its relevance to the development of autoimmunity. Adv Exp Med Biol 181–202 [book chapter review]
- Haji-Ghassemi O, Muller-Loennies S, Rodriguez T, Brade L, Grimmecke HD, Brade H, Evans SV. (2016) The combining sites of anti-lipid antibodies reveal a widely-utilized motif specific for negatively charged groups. J Biol Chem 291: 10104–10118.
- Haji-Ghassemi O, Gilbert M, Spence J, Schur MJ, Parker MJ, Jenkins ML, Burke JE, van Faassen H, Young NM, Evans SV. (2016) Molecular basis for recognition of the cancer glycobiomarker, LacdiNAc (GalNAc[ß1-4]GlcNAc), by Wisteria floribunda Agglutinin. J Biol Chem. 291: 24085–24095.
- Haji-Ghassemi O, Blackler RJ, Martin Young N, Evans SV. (2016) Antibody recognition of carbohydrate epitopes. Glycobiology 25: 920–952. [review article].
- Haji-Ghassemi O, Müller-Loennies S, Rodriguez T, Brade L, Kosma P, Brade H, Evans SV. Structural basis for antibody recognition of lipid a: Insights to polyspecificity toward single stranded DNA. J Biol Chem. 290: 19629–19640.