You are cordially invited to participate in the meeting on Molecular Chaperones and Stress Responses which will be held at Cold Spring Harbor Laboratory, 32 years after the inaugural meeting in this series. The meeting will begin on Tuesday, April 29, 2014, and will conclude with lunch on Saturday, May 3rd. 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.