Ubiquitylation is a reversible protein modification that is implicated in many cellular functions.
Recently, much progress has been made in the characterization of a superfamily of …

Autophagosome formation is a complex process that begins with the nucleation of a pre-autophagosomal
structure (PAS) that expands into a phagophore or isolation membrane, the …

Ubiquitin is a common demoninator in the targeting of substrates to all three major protein
degradation pathways in mammalian cells: the proteasome, the lysosome, and the …

The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases)
maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from …

A proton pump, the vacuolar ATPase, is known to generate the acidic lumenal environment
of endosomes and lysosomes. We have investigated the role of the vacuolar ATPase in …

Ubiquitylation is a major posttranslational modification that controls most complex aspects
of cell physiology. It is reversed through the action of a large family of deubiquitylating …

The JAMM (JAB1/MPN/Mov34 metalloenzyme) motif has been proposed to provide the
active site for isopeptidase activity associated with the Rpn11/POH1 subunit of the 19S-…

Ubiquitination controls the stability of most cellular proteins, and its deregulation contributes
to human diseases including cancer. Deubiquitinases remove ubiquitin from proteins, and …

The proteome of any system is a dynamic entity, such that the intracellular concentration of
a protein is dictated by the relative rates of synthesis and degradation. In this work, we have …

The ubiquitin system is a major coordinator of cellular physiology through regulation of both
protein degradation and signalling pathways. A key building block of a systems-level …