Title:   
Professor

Institute:
University of Western Ontario, London

Department:  
Biochemistry

Province:
Ontario

Training:  
PhD University of Toronto, Toronto, Ontario, Canada
MSc Shanghai institute of Biochemistry and Cell Biology, Chinese Academy of Science, China
BSc Beijing University, Beijing, China

Research interests:
To elucidate the molecular basis of protein-protein interaction and understand how aberrant changes in protein function and connectivity alter cellular behavior and lead to diseases. 

Recognitions:
Canada Research Chair in Functional Genomics and Cellular Proteomics (2010)

Career highlights:
Boehringer Ingelheim (Canada) Young Investigator Award for the Biological Sciences (2004)
Premier’s Research Excellence Award (Government of Ontario) (2001)
Harold E. Johns Award, National Cancer Institute of Canada (2001)

Research Projects

Project title:
Exploring the Cten-DLC1 signaling axis for cancer intervention

Funding period:  
2010-2012

Program:
Operating Grant (Basic Research)

Summary:
Metastasis is initiated by the migration of cancer cells away from the initial site of lesion to invade surrounding tissues. This process of cancer cell migration and invasion is regulated by changes in the actin cytoskeleton, the mechanical framework of a cell.  Many factors can affect actin dynamics and alter cell motility. In breast cancers, abberrant signaling through the epithelial growth factor (EGF) receptor is often associated with poor prognosis.  Although it is known that EGFR signaling contributes to cancer metastasis by promoting cell migration, the underlying molecular mechanism is not fully understood. We found that EGF-induced cell migration is dependent on the protein product of deleted in liver cancer 1 (DLC1), a gene that is deleted or mutated in a wide variety of cancers such as liver, lung, breast and prostate. The proposed research program is focused on understanding the signaling pathways and biochemical basis of DLC1 activation by a group of proteins called tensins. Tensin proteins are key regulators of the actin cytoskeleton, but their expressions are dynamically controlled by EGF. We expect our research to provide novel insights into the molecular basis of cancer metastasis and aid in efforts in exploiting the DLC1-tensin signaling axis for potential cancer intervention.

CRS publications:

Kaneko T, Li L, Li SS. (2008) The SH3 domain--a family of versatile peptide- and protein-recognition module. Front Biosci. 13:4938-52.

Wu C, Ma H, Tseng S-R,  Jia C, Jurisica, I and Li, SS-C (2007) Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening. Proteomics  7:1775-85.

Jia CYH, Nie J, Wu C, Li C. and Li SS-C (2005) Novel specificity of the SH3 domain identified from a proteomic screen of a Pro-rich region. Mol. Cell. Proteomics  4:1155-66.

Li SS-C (2005) Specificity and promiscuity of proline-recognition domains- Structural basis and implications to cellular signaling transduction. Biochem. J.  390:641-53.

Liu Q, Berry D, Nash P, Pawson T, McGlade CJ, and Li SS-C (2003) Structural basis for specific binding of the Gads SH3 domain to an RxxK-motif containing SLP-76 peptide – a novel mode of peptide recognition. Mol. Cell 11:471-481.

Past CRS projects:  
 
2006 Novel functions of the PLCy1 SH3 domain and their relevance to cancer
 
2004 Structural and functional characterization of novel interactions mediated by the PLC-r1 SH3 domain
 
2002 Novel SH3 domain interactions for SLP-76 - A key adaptor protein in T cell development and activation.