Using Ubiquitin Binders to Decipher the Ubiquitin Code

Expanding the Ubiquitin Code

The ubiquitin code.

The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct ...

Ubiquitin code assembly and disassembly

Ubiquitin, a 76 amino-acid polypeptide, presents a compact three-dimensional structure, utilising a fold that recurs within larger polypeptides and in other protein modifiers, such as NEDD8 and SUMO. Ubiquitylation was initially recognised as a signal for proteasome-mediated degradation. We shall consider here how this view has evolved to appreciate that the dynamic appendage of different types...

Engineering ubiquitin to modulate the ubiquitin proteosome system.

Ubiquitination determines the longevity of proteins in cells and plays major roles in signaling. The complexity of the ubiquitination proteasome system (UPS) is evident in the number of enzymes that are involved, including hundreds of ligases and roughly a hundred deubiquitinases (DUBs) that add or remove ubiquitin chains, respectively. Furthermore, ubiquitin modifications on proteins are recog...

Synthesis of Poly-Ubiquitin Chains Using a Bifunctional Ubiquitin Monomer

An optimized large scale and highly reproducible route to orthogonally protected γ-thiolysine is reported. Its utility in the synthesis of bifunctional ubiquitin monomers is demonstrated. These ubiquitin synthons are employed in polymerization reactions giving access to synthetic poly-ubiquitin chains of defined linkage.