Molecular Chaperones & Stress Responses

The meeting will feature advances in the areas of structure and mechanism of action of molecular chaperones; mechanisms of induction of the stress response; the role of chaperones in protein degradation, and chaperone function in disease, development and organellar homeostasis. Chaperones are intimately involved in basic biological processes such as protein translation, folding, complex assembly and disassembly, translocation across membranes and protein degradation.

The contribution of heat shock proteins, to protein folding in vivo across the entire proteome will be described alongside function of specialized chaperones with more limited clientele. The interactions of chaperones and unfolded and misfolded proteins will be discussed in molecular and atomic detail. At the cellular level, the interactions between chaperones in the formation of protein folding networks will be discussed and at the physiological level the impact of altered chaperone buffering capacity on organellar, cellular and organismal function will be discussed.

Sessions:
Protein Folding Machines I
Protein Folding Machines II
Networks
Spatial Quality Control
Diseases
ER
Degradation
Synthesis
Functional Aggregates
+ show speakers and program
Discussion Leaders:
Angelika Amon
Elke Deuerling
Randolph Hampton
Manjit Hayer-Hartl
Linda Hendershot
Ursula Jakob
Harm Kampinga
Rachel Klevit
Susan Lindquist
Richard Morimoto
Thomas Nystrom
Stanley Prusiner
Sheena Radford
Roland Riek
Helen Saibil
Brenda Schulman
Jonathan Weissman

29 Apr - 3 May 2014

Cold Spring Harbor
United States of America
meeting website