Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Professor Mads Gyrd-Hansen reviews the current knowledge about this important post-translational modification.

Ubiquitin is a post-translational modification to proteins that has many cellular functions. Ubiquitin is added to proteins in chains that can be linked together in different ways. A particular type of ubiquitin chain, so-called Met1-linked ubiquitin, is involved in intracellular signalling in response to inflammation and infection. Researchers are trying to understand more about how these Met-1-linked ubiquitin chains are assembled and disassembled to regulate immune signalling and host responses to pathogens, and how they may be targeted therapeutically.

In this review article published in Cell Death and Differentiation, Berthe Katrine Fiil and Ludwig Oxford’s Mads Gyrd-Hansen summarise what is currently known and identify some of the key remaining questions in the field.

Similar stories

Mechanistic insights into the ZBP1 inflammatory response

A collaborative study, led by former Ludwig Oxford group leader Professor Mads Gyrd-Hansen, sheds light on the ZBP1-induced signalling pathway, a pathway which contributes to the viral immune response, including to SARS-CoV-2