Research ResourceProteomics

Hyperplexing: A Method for Higher-Order Multiplexed Quantitative Proteomics Provides a Map of the Dynamic Response to Rapamycin in Yeast

Science Signaling  27 Mar 2012:
Vol. 5, Issue 217, pp. rs2
DOI: 10.1126/scisignal.2002548

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Improving Throughput

Mass spectrometry is a powerful tool for monitoring changes in protein abundance and posttranslational modifications. Dephoure and Gygi describe a mass spectrometry approach that enables the analysis of samples from multiple conditions simultaneously by combining two different labeling methods, which they call “hyperplexing.” Using this method, the authors monitored changes in protein abundance in yeast in response to the drug rapamycin, an inhibitor of the kinase TOR, that has been clinically used as an immunosuppressant and anticancer agent. Rapamycin-induced changes in the abundance of proteins in a six-point time course with biological triplicates were monitored in a single experiment. Statistical analysis provided a high-confidence set of proteins that increased or decreased in abundance in response to this drug. This technique should facilitate the application of quantitative mass spectrometry to the analysis of dynamic cellular events.