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Search Results to Jane McGlade

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overview My research is directed towards understanding the regulation of protein interactions and signal-transduction pathways that control normal cellular functions, and that are disrupted in human disease. Projects in the lab are currently focused on three main themes: phospho-proteomic profiling of tyrosine kinase driven leukaemia; ubiquitin dependent regulation of oncogenic signaling and mechanisms of E3 ligase activity; regulation of alternative splicing by oncogenic signalling and specificity of protein isofom function. Regulation signal transduction by modular adaptor proteins. My colleagues and I have focused the identification and functional characterization of intracellular adapter proteins that function to integrate, localize, and down regulate signal-transduction cascades. My laboratory has cloned and characterized novel adapters that function in antigen-receptor and cytokine signaling (GADS, SLAP), and others that regulate the activity of trans-membrane receptors that determine cell fate and polarity during development (NUMB). Work in my laboratory focuses on detailed molecular and functional characterization of these molecules, including their post translational modifications, isoform specific functions, their associated protein networks and functions in brain and blood cancers. Currently, we are also investigating the developmental signaling and oncogenic pathways that regulate the expression of Numb adaptor isoforms through alternative splicing. Ubiquitin dependent regulation of cell polarity and vesicle trafficking. Our lab is studying the role of ubiquitin in the regulation of signaling pathways and trafficking of surface receptors. We discovered a family of novel PDZ domain containing E3 ubiquitin ligases that includes LNX and LNX2and determined the function of LNX and LNX2 activity in cell fate determination and the establishment of cell polarity during embryonic development. A second small family of E3 ligases currently under investigation by our group includes RNF126 and RabRING7. We have found that these ligases can mediate the formation of both K48 and K63 linked chains and regulate late endosome sorting of receptor tyrosine kinases. Most recently we have discovered a novel mechanism that regulates the ubiquitin ligase activity of CBL and developed in vitro approaches to identify potential therapeutics for diseases that are driven by activated tyrosine kinases. Development of high-throughput functional protein assays and molecular tool archives. In collaboration with Daniela Rotin in the Department of Biochemistry, I developed a Canadian Foundation for Innovation funded functional proteomics program. In the first phase, we assembled the SIDNET Protein Archive of ~14,000 human proteins and developed high throughput assays to measure protein function using protein arrays and high throughput detection and imaging systems. The SIDNET platform capabilities were then expanded to include mouse and human shRNA and esiRNA libraries, and most recently, small molecule and drug libraries. Currently my group is establishing a high throughput assay to identify oncogenic and developmental signaling pathways that regulate alternative splicing events as well as small molecule regulators of ubiquitin ligases. In 2013, SIDNET merged with the Advanced Protein Technology Centre and became the SPARC Biocentre. (http://www.sickkids.ca/Research/SPARC/about-us/index.html)

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