How are linear (Met1) linked polyubiquitin chains cleaved?
| Dates: | 6 June 2014 |
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| Times: | 11:00 - 12:00 |
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| What is it: | Seminar |
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| Organiser: | Faculty of Life Sciences |
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| Speaker: | Paul Elliott |
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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.
Speaker
Paul Elliott
Role: MRC Career Development Fellow
Organisation: MRC Laboratory of Molecular Biology, Cambridge
Travel and Contact Information
Find event
1.006
AV Hill Building
Manchester
