All eukaryotes rely on selective proteolysis to control the abundance of key regulatory
proteins and maintain a healthy and properly functioning proteome. Most of this turnover is …

Proteasomes, the primary mediators of ubiquitin–protein conjugate degradation, are
regulated through complex and poorly understood mechanisms. Here we show that USP14 …

Ubiquitination is a type of post-translational modification that covalently links ubiquitin to a
target protein, which plays a critical role in modulating protein activity, stability, and …

The 20S proteasome functions in protein degradation in eukaryotes together with the 19S
ATPases or in archaea with the homologous PAN ATPase complex. These ATPases contain …

Perturbed cellular protein homeostasis (proteostasis) and mitochondrial dysfunction play an
important role in neurodegenerative diseases, however, the interplay between these two …

Proteins are targeted to the proteasome by the attachment of ubiquitin chains, which are
markedly varied in structure. Three proteasome subunits–Rpn10, Rpn13, and Rpn1–can …

The proteasome is essential for the selective degradation of most cellular proteins, but how
cells maintain adequate amounts of proteasome is unclear. Here we show that there is an …

The linkage, length, and architecture of ubiquitin (Ub) chains are all important variables in
providing tight control over many biological paradigms. There are clear roles for branched …