David Komander becomes our first MRC PPU PhD student to be elected to the Royal Society.

David undertook his PhD studies with Dario Alessi and Daan van Aalten between 2002-2005 characterising the structure, regulation and function of 3-phosphoinositide dependent protein kinase-1 (PDK1).

David was elected to the Royal Society for the important contributions he has made to the understanding of protein ubiquitylation.

He uncovered multiple enzymes and proteins that recognize specific ubiquitin signals helping illuminate some of the remarkable complexity of the ‘Ubiquitin Code’ beyond protein degradation.

David discovered the deubiquitylating enzyme OTULIN, that exclusively cleaves Met1-linked ‘linear’ ubiquitin chains. He revealed that loss of function mutations in OTULIN cause a severe human inflammatory disease and his work suggested new potential treatments for this condition.

David’s lab has also developed numerous methodologies including UbiCRest and Ub-clipping that enable ubiquitin chain architecture and branching to be much better studied.

David also undertook detailed structural analysis of the mitophagy regulators PINK1 and Parkin, advancing our understanding of how these enzymes are regulated and function. This research has helped define how mutations in PINK1 and Parkin impact function resulting in Parkinson’s disease.

Overall, David’s work has helped emphasize the importance of ubiquitin in cellular signalling and human disease. It has laid foundations for improved therapies for diseases such as cancer, inflammation and Parkinson’s disease to be developed.