ERC Consolidator Grant · 2016
Understanding the complexity and architecture in protein ubiquitination
The posttranslational modification of proteins with polyubiquitin regulates virtually all aspects of cell biology. This versatility arises from eight distinct linkage types between individual ubiquitin moieties in polyubiquitin, which co-exist in cells, are independently regulated, and eventually determine the fate of the modified protein. However, ubiquitin chain architecture can be highly complex, and the extent of ‘chain branching’ is unknown. Moreover, ubiquitin also undergoes phosphorylation and acetylation, which can dramatically alter its function. A true appreciation of the complexity in the ubiquitin code can only be achieved when all above aspects are considered, and only then…
From the public funding record at EU CORDIS. Describes the funded project, not the reviews below.