Confirmed keynote speaker:

 

Jim Bardwell, University of Michigan and Howard Hughes Medical Institute

Rowena G. Matthews Collegiate Professor of Molecular, Cellular, and Developmental Biology

Howard Hughes Medical Institute Investigator
University of Michigan, Ann Arbor, USA

 

James Bardwell was born in Saskatoon and did his undergraduate work at the University of Saskatchewan. He did his PhD at the University of Wisconsin-Madison, where working under Elizabeth Craig he discovered homologues to eukaryotic Hsp70 and Hsp90. This provided an early indication that heat shock protein function is both important and conserved. In his postdoc at Harvard Medical School under Jon Beckwith he discovered DsbA and DsbB and through this demonstrated that the formation of disulfides is catalyzed in prokaryotes. As a faculty member and Howard Hughes Investigator at the University of Michigan he devised a selection for optimizing protein stability in vivo. Using this he discovered a new ATP independent chaperone called Spy that inhibits protein aggregation and enhances protein refolding. Using Spy, he has addressed four mysteries of chaperone biology: how chaperones rapidly bind to proteins, how the chaperone-substrate complex is stabilized, how a chaperone can facilitate substrate folding, and what triggers substrate release. He has also devised a novel structural biology approach that enabled him to visualize the dance of chaperone-mediated folding.

 

Confirmed speakers:

 

Leah Cowen, University of Toronto

Heather Durham, McGill University

Julie Forman-Kay, University of Toronto

Kalle Gehring, McGill University

Paul LaPointe, University of Alberta

Christine Vande Velde, University of Montreal

David Vocadlo, Simon Fraser University

Joel Watts, University of Toronto