Title of the presentation:

Sub-cellular proteomics: protein interaction mapping and protein quantitation.

Biography:

Dr Figeys is a Systems Biologist and Analytical Chemist. He is the Director of the Ottawa institute of Systems Biology, University of Ottawa and a Canada Research Chair in Proteomics and Systems Biology.

Short summary of research interests:

Our research efforts are focused on the development and application of proteomics, lipidomics, and technology development.

In proteomics, we are interested in developing and applying techniques for 1) the mapping of protein-protein interactions for proteins relevant to human diseases, and 2) the study of quantitative changes in the proteome when limited amount of material is available.

In lipidomics, we are interested in developing and applying techniques for the study of changes in the lipidome during diseaes. In particular, we are targetting specific subclasses sof lipids such as PC, PE, and PS and are developing techniques for other classes of lipids as well. In collaboration with the laboratory of Dr. S. Bennett we are studying the targetted lipidome in neurodenegrative diseases.

Finally, our technology development efforts are focused on developing proteomics technologies to study minute levels of proteins, the development of lipidomic technologies and the development of bioinformatic tools.

Abstract:

The field of proteomics has rapidly progressed and it is now feasible to routinely identify and quantify 1000's of proteins. The focus of shotgun proteomics has primarily been on the quantitation of protein changes that can be observed at the whole cell/tissue level. However, changes that occur in specific organelles are often missed through this approach as the proteome of the organelle gets buried in the whole cellular proteome. Here, we will discuss application of proteomics at the sub-cellular level. First, we will describe a novel technique, termed modified Chromatin immunopurification (mChIP), for the mapping of the interactions of DNA-bound proteins along with their associated protein network. This approach outperforms conventional protein interactions mapping approaches for DNA associated proteins. Second, we will describe techniques for the quantitative analysis of the proteomic changes at the subcellular levels.