Hsp90 inhibition induces both protein-specific and global changes in the ubiquitinome

We used stable isotope labeling and antibody-based peptide enrichment to quantify more than 1500 protein sites modified with a Gly-Gly motif, the remnant of ubiquitination, in human T-cells treated with an Hsp90 inhibitor. We compared the data with the evolution of net protein levels in the same cells and with changes in protein decay and synthesis rates from a previous study.