FOR 5872 (DFG Research Unit)
Chaperone-mediated regulation of the emergence of disease-causing amyloids inside biomolecular condensates
This DFG research unit investigates how protein misfolding and aggregation in neurodegenerative diseases arise within biomolecular condensates, and how molecular chaperones modulate these processes. The consortium combines expertise in protein biochemistry, chaperone biology, structural biology, biophysics, and condensate research.
Together, the groups will address:
- which protein conformations and interactions drive condensate formation and their conversion into amyloid fibrils;
- how chaperones are recruited to condensates and how they alter the structure and dynamics of TDP-43, Tau, and Huntingtin;
- how chaperones control condensate formation, dissolution, and physical properties;
- how chaperones can prevent the emergence of toxic oligomers and aggregates.
The goal is to build a clear molecular understanding of how condensates and chaperones interact to influence protein misfolding in disease.
Cooperating partners
Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
- Janine Kirstein (Coordinator & Speaker)
Partners
- Simon Alberti (Co-Speaker), TU Dresden, Dresden
- Simon Ebbinghaus, RU Bochum, Bochum
- Mark Hipp, Uni Oldenburg, Oldenburg
- Janine Kirstein, FLI, Jena
- Fan Liu, FMP & Charite, Berlin
- Julia Mahamid, EMBL, Heidelberg
- Rina Rosenzweig, Weizmann Institute of Science, Rehovot
- Christoph Weber, Uni Augsburg, Augsburg
- Susanne Wegmann, DZNE, Berlin
- Markus Zweckstetter, DZNE, Göttingen
