Elucidating protein folding: Mechanisms of folding, misfolding, and intervention in diseases
Description
How do proteins fold correctly and what happens when this process goes wrong? This session reveals the elusive pathways by which α-synuclein transitions from dynamic condensates to toxic fibrils, uncovering key intermediates that drive neurodegeneration in Parkinson's disease. It also highlights how the ribosome actively guides protein folding during synthesis, preventing mis-assembly and ensuring cellular homeostasis. Together, these insights open new opportunities to target misfolding at its earliest stages, offering promising avenues for therapeutic intervention.
The session will include presentation of a FEBS Anniversary Prize of the GBM to speaker David Balchin.
- 9:00 AMStructural pathways of α-synuclein misfolding from condensates to toxic fibrils
- 9:30 AMCharting and disrupting cotranslational folding
- 10:00 AMBag-1S directly binds p97/VCP and decouples ATPase activation from ERAD output
- 10:15 AMDNAJB1 delays Aβ42 aggregation independently of Hsp70 system
- 10:30 AMConformational Landscape and TARP-2 Modulation of GluA4 AMPA Receptors