EPFL BioE Talks SERIES "Protein Quality Control of Stress Granules: Implications in Amyotrophic Lateral Sclerosis"
Event details
| Date | 12.01.2026 |
| Hour | 12:15 › 13:15 |
| Speaker | Prof. Serena Carra, Department of Biomedical, Metabolical and Neurosciences, University of Modena and Reggio Emilia (IT) |
| Location | Online |
| Category | Conferences - Seminars |
| Event Language | English |
WEEKLY EPFL BIOE TALKS SERIES (sandwiches provided)
Abstract:
Wild-type TDP-43 forms cytosolic inclusions in patients afflicted by Amyotrophic Lateral Sclerosis (ALS).
The origin of TDP-43 aggregates and the mechanisms used by cells to counteract TDP-43 aggregation are only partly understood.
Stress conditions trigger the accumulation of TDP-43 in stress granules (SGs), which are dynamic RNA-containing condensates. The role of SGs in modulating TDP-43 aggregation is ambiguous. TDP-43 can misfold and aggregate independently of SGs, but chronic induction of SGs has been shown to trigger the formation of cytosolic TDP-43 inclusions that cause neurotoxicity.
I will present data supporting the role of the protein quality control (PQC) and stress-induced post-translational modifications in preventing protein aggregation inside SGs. Potentiating the PQC of SGs could prevent TDP-43 aggregation during stress.
Bio:
Serena Carra received her PhD in Neurobiology from the University of Catania (Italy) in 2004. After postdoctoral research with Prof. Landry (Laval University, Canada), Prof. Kampinga (University Medical Centre Groningen - UMCG, The Netherlands), she started her independent career in 2009 at UMCG. During this period, Serena discovered the HSPB8-BAG3-HSP70 chaperone complex and its role in targeting misfolded proteins to autophagy for clearance, with implications for neurodegenerative diseases. In 2011, Serena received the Rita Levi Montalcini Prize and moved to the University of Modena and Reggio Emilia, Italy, where she is Associate Professor of Molecular Biology since 2015. Here, she studies how the protein quality control system prevents the aggregation of proteins and maintains the dynamic properties of biomolecular condensates such as stress granules, and how failure thereof contributes to neurodegeneration and neuromuscular disorders.
Zoom link (with one-time registration for the whole series) for attending remotely: https://go.epfl.ch/EPFLBioETalks
Instructions for 1st-year Ph.D. students planning to attend this talk, who are under EDBB’s mandatory seminar attendance rule:
IN CASE you cannot attend in-person in the room, please make sure to
Abstract:
Wild-type TDP-43 forms cytosolic inclusions in patients afflicted by Amyotrophic Lateral Sclerosis (ALS).
The origin of TDP-43 aggregates and the mechanisms used by cells to counteract TDP-43 aggregation are only partly understood.
Stress conditions trigger the accumulation of TDP-43 in stress granules (SGs), which are dynamic RNA-containing condensates. The role of SGs in modulating TDP-43 aggregation is ambiguous. TDP-43 can misfold and aggregate independently of SGs, but chronic induction of SGs has been shown to trigger the formation of cytosolic TDP-43 inclusions that cause neurotoxicity.
I will present data supporting the role of the protein quality control (PQC) and stress-induced post-translational modifications in preventing protein aggregation inside SGs. Potentiating the PQC of SGs could prevent TDP-43 aggregation during stress.
Bio:
Serena Carra received her PhD in Neurobiology from the University of Catania (Italy) in 2004. After postdoctoral research with Prof. Landry (Laval University, Canada), Prof. Kampinga (University Medical Centre Groningen - UMCG, The Netherlands), she started her independent career in 2009 at UMCG. During this period, Serena discovered the HSPB8-BAG3-HSP70 chaperone complex and its role in targeting misfolded proteins to autophagy for clearance, with implications for neurodegenerative diseases. In 2011, Serena received the Rita Levi Montalcini Prize and moved to the University of Modena and Reggio Emilia, Italy, where she is Associate Professor of Molecular Biology since 2015. Here, she studies how the protein quality control system prevents the aggregation of proteins and maintains the dynamic properties of biomolecular condensates such as stress granules, and how failure thereof contributes to neurodegeneration and neuromuscular disorders.
Zoom link (with one-time registration for the whole series) for attending remotely: https://go.epfl.ch/EPFLBioETalks
Instructions for 1st-year Ph.D. students planning to attend this talk, who are under EDBB’s mandatory seminar attendance rule:
IN CASE you cannot attend in-person in the room, please make sure to
- send D. Reinhard a note well ahead of time (ideally before seminar day), informing that you plan to attend the talk online, and, during seminar:
- be signed in on Zoom with a recognizable user name (not any alias making it difficult or impossible to identify you).
Practical information
- Informed public
- Registration required
Organizer
- Prof. Paolo De Los Rios, Institute of Physics & Institute of Bioengineering
Contact
- Institute of Bioengineering (IBI), Dietrich REINHARD