|Degrees:||B.Sc. (St. Francis Xavier), Ph.D. (Carleton)|
|Phone:||613-520-2600 x 4487|
|Office:||Office: 248 Nesbitt Building|
|Website:||Visit my lab website|
My lab is primarily interested in the discovery and characterization of how proteins coordinate and work together to achieve a particular cellular function, this is often referred to as functional proteomics. This includes how proteins dynamically interact with each other, how enzymes select substrates, as well as working to define the changes in protein signaling, or regulatory networks, that accompany disease progression or resistance to treatment. Specifically, my research focuses on reversible modifications made to proteins, called post-translational modifications (PTMs), and how lysine methylation PTM regulates protein-protein interactions and function. My lab also has experience with (1) mapping the substrate selection of enzymes, and (2) binding preferences of an interacting protein in order to create larger networks of protein interaction. This research is facilitated by using advanced biochemical and molecular biology techniques that include the synthesis of custom peptide arrays and implementation functional proteomic technologies in the screening of protein-protein and enzyme-substrate interactions. Students in my lab will be able to gain valuable experiences in both basic and advanced cellular and biochemical methods, and engage in interdisciplinary collaborative opportunities.
I am currently seeking students to join the lab. Positions are available at all levels, including undergraduate, Honour’s, MSc, and PhD. Research projects include “the role of dynamic methylation in adapting cells to low oxygen” and “expanding the enzyme-substrate networks of methyltransferase enzymes”. Depending on the project and interests of the student, most will involve molecular cloning, mammalian tissue culture, protein expression, protein-protein interaction, functional assays, and bioinformatics.
Biggar KK, Li SSC. (2015). Non-histone protein methylation as a regulator of cellular signalling and function. Nature Reviews Molecular Cell Biology 16(1): 5-17.
Biggar KK, Dawson NJ, Storey KB. (2013). Proteomic characterization of fructose-1,6-bisphosphate aldolase from anoxia tolerance Trachemys scripta elegans: Bioinformatics and mass spectrometric exploration of enzymatic activity. PLoS ONE 8(7): e68830.
Biggar KK, Dawson N, Storey KB. (2012). Real-time protein unfolding: a method for determining the kinetics of native protein denaturation using a qRT thermocycler. Biotechniques 53(4): 231-238.
Malkani N, Biggar KK, Shehab MA, Li SSC, Jansson T, Gupta MB. (2015). IGFBP-1 hyperphosphorylation induced by leucine deprivation is mediated by CK2 and PKC. Molecular Endocrinology 30(2): 201-2016.
Schaap P, Barrantes I, Minx P, Anderson RW, Bénard M, Biggar KK, Buchler N, Bundschuh R, Chen X, Fronick, C, Fulton L, Golderer G, Gott J, Jahn N, Knoop V, Landweber L, Maric C, Miller D, Noegel A, Peace R, Pierron G, Sasaki N, Sasaki T, Schallenbarg-Rüdinger M, Schleicher M, Singh R, Spaller T, Storey KB, Suzuki T, Tomlinson T, Tyson JJ, Warren W, Werner ER, Werner-Felmayer G, Wilson RK, Winckler T, Gott J, Glöckner G, Marwan W. (2016). The Physarum polycephalum genome reveals extensive use of prokaryotic two-component and metazoan-type tyrosine kinase signaling. Genome Biology and Evolution 8(1): 109-125.