Proper expression, folding, transport, and clearance of proteins are critical for cell function and organismal health. Chaperones and enzymes that post-translationally assist newly synthesized proteins help ensure that they are correctly folded and functional, or are degraded. Translocation machineries, proteasomes, and autophagic activities are critical for subcellular localization and for degradation as necessary. Stress and aging challenge the robustness of these chaperone and clearance networks leading to protein mismanagement, overload, and cellular dysfunction. In humans, this is associated with the accumulation and aggregation of misfolded and aggregation-prone proteins, a feature of numerous neurodegenerative, metabolic, and oncogenic diseases.

You are invited to participate in the 2016 meeting on Protein Homeostasis in Health & Disease, marking the 25th anniversary of the first Cold Spring Harbor meeting in 1991 related to heat shock and the role of molecular chaperones. Over the past twenty-five years, the field has exploded and much groundbreaking work - on molecular chaperones, the unfolded protein response, stress responses, and how these processes are implicated in disease - has first been presented at this meeting. This year's meeting provides an opportunity to showcase the latest research in this area and to feature several keynote talks by leading investigators who have contributed to the development of the field and who will put their current efforts in the context of past developments.

The meeting will begin after dinner at 7:30 p.m. on Monday, April 18, and conclude with lunch on Friday, April 22, 2016.