Proteomics

Dataset Information

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

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell, Cell Culture

SUBMITTER: Manfredo Quadroni  

LAB HEAD: Manfredo Quadroni

PROVIDER: PXD001549 | Pride | 2015-03-19

REPOSITORIES: Pride

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MaxQuant_output.zip Other
UB_GA_analysis.zip Other
UB_GA_silac.zip Other
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Publications

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

Quadroni Manfredo M   Potts Alexandra A   Waridel Patrice P  

Journal of proteomics 20150314

Inhibition of the essential chaperone Hsp90 with drugs causes a global perturbation of protein folding and the depletion of direct substrates of Hsp90, also called clients. Ubiquitination and proteasomal degradation play a key role in cellular stress responses, but the impact of Hsp90 inhibition on the ubiquitinome has not been characterized on a global scale. We used stable isotope labeling and antibody-based peptide enrichment to quantify more than 1500 protein sites modified with a Gly-Gly mo  ...[more]