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 16th meeting on Protein Homeostasis in Health & Disease. 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 over the past three decades plus. The 2024 meeting provides an opportunity to showcase the latest research in this area and will feature talks by leading investigators.
The meeting will begin after dinner at 7:30 p.m. on Wednesday, April 24, and conclude with lunch on Sunday, April 28, 2024.