Functional Proteomics by Induced Proximity
Event details
| Date | 24.06.2024 |
| Hour | 14:30 › 15:30 |
| Speaker | Prof. Mikko Taipale, Donnelly Centre for Cellular and Biomedical Research, University of Toronto (CAN) |
| Location | Online |
| Category | Conferences - Seminars |
| Event Language | English |
BIOENGINEERING SEMINAR
Abstract:
Targeted protein degradation and stabilization are promising therapeutic modalities due to their potency, versatility, and potential to expand the druggable target space. However, only few E3 ligases and DUBs have been harnessed for this purpose, significantly limiting the potential of the approach. Moreover, there may be other protein classes that could be exploited for this purpose. We established a synthetic proteome-scale platform to functionally identify human proteins that can promote the degradation or stabilization of a target in a proximity-dependent manner. Our results reveal that the human proteome contains a large cache of effectors of protein stability, many of which are more potent than proteins currently exploited for targeted protein degradation and stabilization. More generally, our study highlights proteome-scale induced proximity screens as a powerful platform for functional proteomics.
Bio:
Mikko Taipale is an Associate Professor in the Donnelly Centre and the Department of Molecular Genetics at the University of Toronto. He received his MSc in genetics at the University of Oulu, Finland (close to the arctic circle). He then joined Asifa Akhtar’s lab in EMBL in Heidelberg, Germany and completed his PhD on chromatin regulation by histone acetylation. He did his postdoctoral training in Sue Lindquist’s lab at the Whitehead Institute. There, he focused on the client recognition mechanisms of Hsp90 chaperone and co-chaperones and on developing high-throughput protein/protein and drug/target interactions. Since 2014, Mikko has had his lab in the Donnelly Centre and the University of Toronto. The Taipale lab is focused on diverse aspects of functional proteomics and genomics, including protein homeostasis, transcriptional regulation, disease variant phenotyping, and host/pathogen interactions.
Zoom link for attending remotely: https://epfl.zoom.us/j/63856907146
Abstract:
Targeted protein degradation and stabilization are promising therapeutic modalities due to their potency, versatility, and potential to expand the druggable target space. However, only few E3 ligases and DUBs have been harnessed for this purpose, significantly limiting the potential of the approach. Moreover, there may be other protein classes that could be exploited for this purpose. We established a synthetic proteome-scale platform to functionally identify human proteins that can promote the degradation or stabilization of a target in a proximity-dependent manner. Our results reveal that the human proteome contains a large cache of effectors of protein stability, many of which are more potent than proteins currently exploited for targeted protein degradation and stabilization. More generally, our study highlights proteome-scale induced proximity screens as a powerful platform for functional proteomics.
Bio:
Mikko Taipale is an Associate Professor in the Donnelly Centre and the Department of Molecular Genetics at the University of Toronto. He received his MSc in genetics at the University of Oulu, Finland (close to the arctic circle). He then joined Asifa Akhtar’s lab in EMBL in Heidelberg, Germany and completed his PhD on chromatin regulation by histone acetylation. He did his postdoctoral training in Sue Lindquist’s lab at the Whitehead Institute. There, he focused on the client recognition mechanisms of Hsp90 chaperone and co-chaperones and on developing high-throughput protein/protein and drug/target interactions. Since 2014, Mikko has had his lab in the Donnelly Centre and the University of Toronto. The Taipale lab is focused on diverse aspects of functional proteomics and genomics, including protein homeostasis, transcriptional regulation, disease variant phenotyping, and host/pathogen interactions.
Zoom link for attending remotely: https://epfl.zoom.us/j/63856907146
Practical information
- Informed public
- Free
Organizer
- Prof. Bruno Correia, Laboratory of Protein Design and Immunoengineering (LPDI), Institute of Bioengineering (IBI), École polytechnique fédérale de Lausanne (EPFL)
Contact
- Ms. Suzanne Balharry, Laboratory of Protein Design and Immunoengineering (LPDI), Institute of Bioengineering (IBI), École polytechnique fédérale de Lausanne (EPFL)