Suzanne Elsasser

TL;DR: It is shown that USP14, a proteasome-associated deubiquitinating enzyme, can inhibit the degradation of ubiquitin–protein conjugates both in vitro and in cells.

TL;DR: The identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome, is reported, suggesting a coupling of chain recognition and disassembly at the prote asome.

TL;DR: It is shown that Rad23 binds proteasomes by directly interacting with the base subcomplex of the regulatory particle of the proteasome, and it is proposed that the LRR domain of Rpn1 may be positioned in the base to allow the cargo proteins carried by Rad23 to be presented to the proteAsomal ATPases for unfolding.

TL;DR: A reconstituted system and quantitative mass spectrometry are used to demonstrate that cyclin B1 is modified by ubiquitin chains of complex topology, rather than by homogeneous Lys 48-linked chains, and provide unique insights into the mechanisms of substrate ubiquitination.

TL;DR: The intimate interplay between the proteasome and Cdc48, mediated in part by loosely associated ubiquitin receptors, has important functions in cellular regulation.