Abstract 2369 Quantitative Proteomics of Mutations in Yeast Hsp90 and Cdc37 Reveal Client Specific Effects

The molecular chaperone Hsp90 and its cochaperone Cdc37 are both essential proteins critical for the folding of hundreds of client proteins, including protein kinases involved in cancer progression, making it a therapeutic target. However, how do Hsp90 and its co-chaperone Cdc37 influence the stability and abundance of their client proteins on a proteome-wide scale? In our first study, we took advantage of yeast genetics and employed Data-Independent Acquisition Mass Spectrometry (DIA-MS) to study nine temperature-sensitive Hsp90 mutants that disrupt distinct phases of its folding cycle.