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

Roscoff (Bretagne), France, October 12-16, 2020
Deadline for application: June 12, 2020

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.