An exciting recent development in cell biology is the increasing number of findings that directly implicate molecular chaperones in protein degradation, thus underscoring the significance of folding and unfolding for proteolysis. However, only few researchers have begun to assess the role of molecular chaperones in proteolysis and the mechanisms by which the cellular machineries for folding and degradation interact are largely unknown. To understand these interactions is of fundamental biological significance and also of medical relevance, as aberrant folding reactions followed by degradation have emerged as the cause of a number of inherited diseases, cystic fibrosis being the most prominent example. It is therefore particularly timely to hold the first international conference that will focus specifically on the interface between protein folding and degradation.
The aim of this meeting is to bring together experts in the fields of chaperone-assisted and unassisted protein folding, protein degradation and protein structure, and to provide scientists from these as well as related disciplines with a forum to discuss emerging mechanistic principles. Because of its multi-disciplinary nature, this conference is expected to define important new research problems and thus should be of considerable interest to the large number of students and postdocs working in traditionally separate fields. Sessions will cover the structure and mechanisms of action of the major chaperone and protease systems, the functional interplay of chaperones and proteases, ubiquitin-dependent degradation, regulation by proteolysis, and recent progress in how to manipulate both chaperones and proteases pharmacologically. In addition the program will include shared sessions with a parallel conference covering protein folding and degradation in the secretory pathway.
