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The University of Western Ontario
The Schulich School Of Medicine & Dentistry
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Department of Biochemistry • Siebens-Drake Research Institute
21 / 11 / 2009
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Predicting protein-protein interactions
Welcome to the Li Lab

The main focus of the Li laboratory is to elucidate the molecular basis of protein-protein interaction and understand how aberrant changes in protein function and connectivity alter cellular behaviour and lead to diseases.

Dr. Li
We use an integrated approach that combines molecular, cellular, and proteomic information to obtain a comprehensive picture of how certain proteins interact and transduce signals in a cell. We are particularly interested in understanding the mechanisms of asymmetric cell division, cell polarity and adhesion, and how adaptor proteins function in facilitating immunoreceptor signaling. Moreover, we employ peptide and protein arrays to identify protein-protein interaction networks underlying these important biological events.
 
A model for the role of Numb in regulating the early events in an epithelial-tomesenchymal transition
Friday, 11 September 2009 06:01

A model for the role of NumbIn epithelial cells under a physiological condition, Numb is involved in stabilization of cell-cell adhesions by binding to E-cadherin or binding to the Par complex via Par3. Upon HGF engagement of the c-Met receptor, one of the downstream components, the c-Src kinase is activated, which leads to tyrosine phosphorylation of E-cadherin (presumably on the YYY triad) and the decoupling of Numb from phospho-E-cadherin consequently. In the meantime, Numb sequesters phosphorylated aPKC and Par6 but releases Par3. The NumbaPKC-Par6 complex may be retained on the plasma membrane or in the cytosol, while Par3 is translocated into the nucleus.

Last Updated ( Friday, 11 September 2009 06:14 )
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The XLP syndrome protein SAP interacts with SH3 proteins to regulate T cell signaling and proliferation
Tuesday, 09 December 2008 15:39

The gene sap/shd1a, which encodes a 128-residue SH2 domain protein, is frequently deleted or mutated in the X-linked lymphoproliferative syndrome (XLP). The SAP SH2 domain differs from others in the same class in that it is not only capable of binding to a phosphotyrosine-containing peptide, it can also associate with an SH3 domain using a distinct surface. This novel mode of ligand-binding is initially discovered in the SLAM-SAP-Fyn complex that plays a critical role in T cell and natural killer cell activation.

Last Updated ( Friday, 11 September 2009 06:15 )
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