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Protein phase transitions in ageing and age-related diseases: from atomic resolution to cellular solutions

The conference
Cells and organisms maintain protein homeostasis in several cooperating ways, which include protein folding, degradation, and sequestration. During aging, the capacity to maintain protein homeostasis declines, which leads to the accumulation of aggregation-prone proteins. These aggregation-prone proteins can accelerate aging and cause age-related diseases like Parkinson’s disease, tauopathies, Alzheimer’s, and Amyotrophic Lateral Sclerosis. How they do so is still not fully understood. Understanding the underlying mechanisms will be important for the development of therapeutic strategies. Recent groundbreaking discoveries have revealed new aspects of protein homeostatic and pathological mechanisms. These include the phenomena of protein phase transitions in membrane-less organelles and the existence of amyloid polymorphisms that are associated with protein toxicity. These phenomena are shared by a range of stress and age-related conditions. This Jacques Monod meeting will highlight these phenomenon, including the biological mechanisms and structural features involved. New findings will be presented by scientists that pioneered the research in these areas. Regulation of both physiological and disease-related transitions will be addressed as well as perspectives on biomedical applications.

The meeting will bring together leading experts in the fields of structural biology, cell biology, physiology and medical biology. It aims to foster exchange of knowledge across these fields and to stimulate interdisciplinary collaboration to further advance the filed.

 

Chairperson: Ellen Nollen
European Research Institute for the Biology of Aging, University Medical Center Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands
Phone: +31 6 52724881
Email: e.a.a.nollen@umcg.nl

Vice-chairperson: Ronald Melki
Laboratory of Neurodegenerative Diseases, CNRS, Institut Francois Jacob (MIRCen), CEA, 18 Route du Panorama, 92265 Fontenay-Aux-Roses cedex, France
Phone: +33 (0)1 46 54 93 78
Email: ronald.melki@cnrs.fr

 

Invited speakers (provisional titles)
Séverine Boillee (Sorbonne Universités, Paris, France)
Modifying factors in ALS

Anja Böckmann (Université de Lyon, Lyon, France)
Structural conversions to amyloid

Luc Buée (Inserm, Lille, France)
Tau physiology

Bernd Bukau (Heidelberg University, Heidelberg, Germany)
Chaperone assisted folding and disaggregation

Serena Carra (University of Modena and Reggio Emilia, Modena, Italy)
Phase transitions in stress granule formation

Matthew R. Chapman (Washington University, St. Louis, USA)
Regulation of bacterial amyloid

Ehud Cohen (Hebrew University, Jeruzalem, Israel)
Metabolic regulation of protein homeostasis

Olga Corti (Sorbonne Universités, Paris, France)
Regulation of mitophagy

Luc Depuis (Université de Strasbourg, Strasbourg, France)
Cellular mechanisms of ALS

Michel Goedert (MRC, Cambridge, United Kingdom)
Molecular mechanisms of Neurodegeneration

Sandrine Humbert (University Grenoble Alpes, Grenoble, France)
Biology of huntingtin

Stéphane Hunot (Sorbonne Universités, Paris, France)
Cellular responses to misfolded proteins

Dan Jarosz (Stanford University, Stanford, USA)
Protein aggregation in health, disease and aging

Jeff Kelly (The Scripps Research Institute, La Jolla, USA)
Therapeutic strategies for systemic amyloidosis

Cynthia Kenyon (University of California, San Francisco, USA)
Protein homeostasis in aging

Janine Kirstein (University of Bremen, Germany)
Disaggregating chaperones

Sylvain Lehmann (Inserm, Montpellier, France)
Biomarkers of Alzheimer’s disease

Sara Linse (Lund University, Lund, Sweden)
Aggregation modifying factors

Ronald Melki (CNRS, Fontenay-aux-Roses, France)
Fibril polymorphisms and propagation

Ellen Nollen (ERIBA, Groningen, The Netherlands)
Cellular modifiers of protein toxicity

Paola Picotti (ETH Zurich, Zurich, Switzerland)
Proteome wide structural changes

Magdalena Polymenidou (University of Zurich, Zurich, Switzerland)
TDP-43 polymorphisms in disease

David Rubinsztein (University of Cambridge, Cambridge, United Kingdom)
Autophagy in health, aging and disease

Henning Stahlberg (University of Basel, Basel, Switzerland)
Amyloid polymorphisms

Paul J Taylor (St Jude Children’s Research Hospital, Memphis, USA)
Phase transitions in neurodegenerative disease

Robert Tycko (National Institutes of Health, Bethesda, USA)
Structural variation in amyloid and phase separation