How are linear (Met1) linked polyubiquitin chains cleaved?
|Starts:||11:00 6 Jun 2014|
|Ends:||12:00 6 Jun 2014|
|What is it:||Seminar|
|Organiser:||Faculty of Life Sciences|
Until recently Met1-linked polyubiquitin was only regarded as providing the source of the cellular ubiquitin pool as ubiquitin is translated as a polyprotien and is post-translationally processed by dedicated deubiquitinating enzymes (DUBs). However, the identification and characterisation of a multi subunit enzyme complex (Linear Ubiquitin Chain Assembly Complex, LUBAC), which assembles Met1-linked polyubiquitin chains and the identification of substrates that are post-translationally modified with Met1-linked chains, particularly during inflammatory signalling responses, has highlighted how Met1-linked polyubiquitin is an important post-translational modifier. The DUB that was responsible for hydrolysing Met1-linked chains in this context had not been identified. I will discuss our work on the Met1-specific DUB, OTULIN and how OTULIN achieves the unique specificity in only hydrolysing Met1-linked ubiquitin chains. Furthermore, I will discuss how OTULIN forms an integral part of the LUBAC signalling complex and the consequences and regulation of such an interaction.
Role: MRC Career Development Fellow
Organisation: MRC Laboratory of Molecular Biology, Cambridge
Travel and Contact Information
AV Hill Building