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Soon after the identification of tyrosine phosphorylation by the v-src tyrosine kinase in the late 1970’s, it became clear that a significant number of key proteins were phosphorylated on tyrosine residues. Interestingly the rapid turnover of phosphate on tyrosine strongly suggested that there were one or more enzymes that performed this dephosphorylating activity.

My laboratory investigates biological functions of several PTPases and their implications in human diseases. PTP1B, TC-PTP, PTP-PEST, RPTP-sigma and PRL-PTPs are the main focus of our research program. In addition, we are developing several new directions in PTP inhibitions as well as in large gene family screens by siRNA of the PTPases in order to find potential applications in various diseases (diabetes, obesity, spinal cord injury, neural degenerative diseases, intestinal bowel diseases and other inflammatory diseases) and particularly in human cancers. Finally, our work has brought us to study the role of PTPases and other genes in the initiation and development of wasting syndrome in cancer cachexia. This latest project is also supported by our effort to characterize the implication of PTPases in cell and organism metabolisms. Our objective is to validate PTPases as genuine targets in human diseases and to bring novel clinical applications based on PTPase biology and pharmacology.

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PTP101
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