The viability of cells, tissues and organisms critically depend on the ability to maintain protein homeostasis (proteostasis) and thus, they constantly adapt the cellular proteome to external and internal alterations. Such alterations include changing environmental conditions, different developmental stages, acute stress such as elevated temperatures, inflammation and oxidative stress, or chronic stress caused by mutations or aging. All these incidents constitute risk factors that provoke a loss of cellular homeostasis that can lead to protein misfolding and aggregation and, eventually, cell death. Such a decline in proteostasis is especially prominent during aging and for a number of diseases including neurodegeneration, cancer, cardiovascular, or metabolic disorders (e.g., diabetes). Thus, the ability of cells to sense and respond to changing conditions and stress is critical for normal cell growth and development, and helps to protect against aging- related diseases. A growing body of evidence shows that cells activate elaborated stress responses to adapt to changing conditions including specific signaling regimes, a complex transcriptional and translational reprogramming, and the activation of cellular quality control systems such as proteolytic pathways and molecular chaperones to prevent accumulation of toxic misfolded and aggregated proteins known to play a critical role in life-span regulation and aging-related disorders such as Alzheimer?s, Parkinson?s, Huntington?s diseases as well as prion-based disease. The 2019 Gordon Research Conference on Stress Proteins in Growth, Development and Disease held in June 23-28, 2019, at the Renaissance Tuscany Il Ciocco in Italy is the tenth in this successful series and will highlight most recent cutting-edge advances in the field of cell stress biology, ranging from underlying basic mechanisms of stress programs and of protein quality control systems up to intervention strategies. Special emphasis will be placed on novel aspects regarding stress signaling and regulation of gene expression, phase separation and other specific deposits of RNA and proteins under stress, elimination strategies of toxic protein species, and the role of organelle stress responses to pathology. Additionally, we will continue recent successful meeting innovations: the Gordon Research Seminar (GRS) will be added from June 22-23, immediately preceding the GRC, to promote the development of early career scientists (PhD students and post-docs) in the field. Poster previews, career roundtable discussions and a ?power hour? focused on women investigators will complete this conference. The formal scientific program, limited attendance, and organized but informal opportunities for interaction make this meeting a pre-eminent conference at the forefront of science promoting a deeper understanding of the impact of stress proteins in human health, aging and disease and the development of efficient countermeasures. The chair is Elke Deuerling (Univ. of Konstanz, Germany) and the vice-chair is Brain C. Freeman (Univ. of Illinois, USA).

Public Health Relevance

The viability, growth and development of cells, tissues and whole organisms critically depends on their ability to maintain proteostasis by adapting the cellular proteome to external and internal alterations and stress. Major defects in maintaining proteostasis are linked to neurodegenerative disorders, such as Alzheimer?s, Huntington?s, and Parkinson?s diseases and are thought to be one of the underlying causes of aging. This conference will have a major impact on broadening our current understanding of the vital role of stress proteins in human health, aging, and disease, and will pave the way to the design of therapeutic strategies to combat aging-related diseases and offer students and junior investigators customized training and networking opportunities.

National Institute of Health (NIH)
National Institute on Aging (NIA)
Conference (R13)
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Neuroscience of Aging Review Committee (NIA)
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Wise, Bradley C
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Gordon Research Conferences
West Kingston
United States
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