Eric J. Bennett

TL;DR: The human ubiquitin-modified proteome is characterized using a monoclonal antibody that recognizes diglycine (diGly)-containing isopeptides following trypsin digestion and it is demonstrated that quantitative diGly proteomics can be utilized to identify substrates for cullin-RING ubiquitIn ligases.

TL;DR: A global proteomic analysis of Dubs and their associated protein complexes provided the first glimpse into the Dub interaction landscape, places previously unstudied Dubs within putative biological pathways, and identifies previously unknown interactions and protein complexes involved in this increasingly important arm of the ubiquitin-proteasome pathway.

TL;DR: Stress granules (SGs) are transient ribonucleoprotein (RNP) aggregates that form during cellular stress and are increasingly implicated in human neurodegeneration as mentioned in this paper.

TL;DR: A mass-spectrometry-based method is exploited to quantify polyubiquitin chains and it is demonstrated that the abundance of these chains is a faithful endogenous biomarker of UPS function, establishing that UPS dysfunction is a consistent feature of HD pathology.

TL;DR: It is reported that production of protein aggregates specifically targeted to either the nucleus or cytosol leads to global impairment of UPS function in both cellular compartments and is independent of sequestration of aggregates into cytoplasmic inclusion bodies (IBs).