The PIDDosome is often used as the alias for a multi-protein complex that includes the p53-induced death domain protein 1 (PIDD1), the bipartite linker protein CRADD (also known as RAIDD) and the pro-form of an endopeptidase belonging to the caspase family, i.e. caspase-2. Yet, PIDD1 variants can also interact with a number of other proteins that include RIPK1 (also known as RIP1) and IKBKG (also known as NEMO), PCNA and RFC5, as well as nucleolar components such as NPM1 or NCL. This promiscuity in protein binding is facilitated mainly by autoprocessing of the full-length protein into various fragments that contain different structural domains. As a result, multiple responses can be mediated by protein complexes that contain a PIDD1 domain. This suggests that PIDD1 acts as an integrator for multiple types of stress that need instant attention. Examples are various types of DNA lesion but also the presence of extra centrosomes that can foster aneuploidy and, ultimately, promote DNA damage. I will discuss the role of PIDD1 in response to DNA damage and highlight novel functions in centrosome surveillance and scheduled polyploidisation during organogenesis.
Date: 1 March 2018, 11:00 (Thursday, 7th week, Hilary 2018)
Venue: NDM Building, Headington OX3 7FZ
Venue Details: Basement seminar room, TDI
Speaker: Dr Andreas Villunger (University of Innsbruck)
Organising department: Ludwig Institute for Cancer Research, Oxford Branch
Organiser: Christina Woodward (Oxford Ludwig Institute, Nuffield Department of Medicine, University of Oxford)
Organiser contact email address:
Host: Dr Mads Gyrd Hansen (Ludwig Cancer Research)
Part of: Ludwig Institute Seminar Series
Booking required?: Not required
Audience: Members of the University only
Editor: Christina Woodward