Michel L. Tremblay
Professor
Microbiology & Immunology
McGill University
Canada
Biography
Protein Tyrosine Phosphatases (PTPases) have been implicated in a variety of cellular processes such as cell growth, differentiation, and cancer. The nature of these enzymes suggests that they may be involved in cancer by acting either as anti-oncogenes or as oncogenes themselves. There is also evidence to suggest that PTPases are involved in mammalian development.
Research Interest
Our research interest has focused on three recently cloned enzymes and their relationship to mouse development and cancer. One of these PTPases, termed MPTP, is a ubiquitously expressed PTPase which localizes to the cell nucleus and may play a role in cell cycle events. MPTP-PEST is a ubiquitously expressed cytosolic enzyme which has been implicated in intracellular signal transduction. PTP NU-3 is a neuronal-cell specific PTPase which belongs to the receptor-type family of enzymes and is thought to play a role in neurogenesis by interacting with the extracellular matrix.
Publications
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Protein tyrosine phosphatase σ regulates autoimmune encephalomyelitis development. Ohtake Y, Kong W, Hussain R, Horiuchi M, Tremblay ML, Ganea D, Li S.
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PRL2 links magnesium flux and sex-dependent circadian metabolic rhythms. Uetani N, Hardy S, Gravel SP, Kiessling S, Pietrobon A, Wong NN, Chénard V, Cermakian N, St-Pierre J, Tremblay ML.
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Downregulation of PTP1B and TC-PTP phosphatases potentiate dendritic cell-based immunotherapy through IL-12/IFNγ signaling. Penafuerte C, Feldhammer M, Mills JR, Vinette V, Pike KA, Hall A, Migon E, Karsenty G, Pelletier J, Zogopoulos G, Tremblay ML.
