Regulation of cullin–RING ubiquitin ligases: the adaptive exchange hypothesis
Event details
| Date | 10.11.2016 |
| Hour | 16:15 › 17:30 |
| Speaker | Prof. Ray Deshaies, Caltech, USA |
| Location | |
| Category | Conferences - Seminars |
Cullin–RING ubiquitin ligases (CRLs) comprise a family of hundreds of enzymes that regulate many aspects of eukaryotic biology ranging from circadian rhythms to glutamine synthesis. Mutations in specific CRLs predispose to leukemia, kidney, and colon cancers, among other diseases. In addition, one particular CRL is the key target of drugs commonly used to treat multiple myeloma. Given their broad impact on biology, we have been interested in understanding how these enzymes work and how they are regulated. In my talk I will focus on regulation of these enzymes by dynamic cycles of assembly and disassembly. Each subfamily of CRLs comprises a common cullin–RING core shared by a group of substrate receptors. For the SCF subfamily of CRLs, the substrate receptors are F-box proteins. The human genome encodes ~70 different F-box proteins. I will describe the ‘Adaptive Exchange’ hypothesis, which posits that the assembly of F-box proteins into SCF complexes is regulated by the presence of their cognate substrates, such that the population of SCF complexes that exists at a given time in a cell is a reflection of the substrates being generated in that cell. This hypothesis has important implications for remodeling of the ‘CRLome’ in response to environmental and developmental signals, and for evolution of the family of CRL enzymes
Practical information
- General public
- Free
Organizer
- Prof. Beat Fierz
Contact
- Marie Munoz