Steven P. Gygi

TL;DR: A straightforward approach is reported to increase the multiplexing capacity of quantitative mass spectrometry, which provides a platform for the analysis of cellular signaling pathways.

TL;DR: A proteomics approach for protein-protein interactions reveals new components of a conserved cell signaling pathway, and selects for further characterization a new member of the alpha-arrestin family, Leash, and shows that it promotes degradation of Yki through the lysosomal pathway.

TL;DR: It is shown that mammalian 26S proteasomes have five associated ubiquitin ligases and that multiple proteasome subunits are ubiquitinated in cells, especially the ubiquit in receptor subunit, Rpn13, which strongly decreases the prote asome's ability to bind and degrade ubiqu itin‐conjugated proteins, but not its activity against peptide substrates.

TL;DR: Improving depth of coverage - measuring abundance changes of over 5000 proteins - increases the understanding of difficult-to-study genes in the model system S. cerevisiae and offers a hypothesis-generating resource for targeted studies on uncharacterized genes.

TL;DR: Insight is provided into GPCR regulation, the functional scope of prolyl hydroxylation is broadened, and the understanding of the cellular response to hypoxia is expanded.