Protein phase transitions in ageing and age-related diseases: from atomic resolution to cellular solutions
Due to the current health situation, the conference is postponed
New date : Roscoff (Bretagne), France, October 18-22, 2021
Deadline for application: To be determined
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
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.
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
Registration
Deadline for application: June 12, 2020
Registration fee (including board and lodging)
460 € for PhD students
750 € for other participants
Application for registration
The total number of participants is limited to 115 and all participants are expected to attend for the whole duration of the conference. Selection is made on the basis of the affinity of potential participants with the topics of the conference. Scientists and PhD Students interested in the meeting should deposit online before the deadline: https://cjm4-2020.sciencesconf.org/
- their curriculum vitae
- the list of their main publications for the 3 last years
- the abstract of their presentation:
The abstract must respect the following template: TemplateResumeFile
- First line: title
- Second line: list of authors. Presenting author underlined
- Third line: author's addresses
- Fourth line: e-mail of the presenting author
Abstracts should be no longer than an A4 page and preferably be submitted in Times New Roman, font size 10 pts. No figures. ".docx" file format.
After the deadline, the organizers will select the participants. Except in some particular cases approved by the Chairperson, it is recommended that all selected participants present their work during the conference, either in poster form or by a brief in- session talk. The organizers choose the form in which the presentations are made. No payment will be sent with application. Information on how and when to pay will be mailed in due time to those selected.