Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Subscribe

Sci. Signal., 27 March 2012
Vol. 5, Issue 217, p. rs2
[DOI: 10.1126/scisignal.2002548]

RESEARCH RESOURCES

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

Noah Dephoure and Steven P. Gygi*

Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

Abstract: Large-scale quantitative proteomics can provide a near-global view of cellular protein abundance. Yet, the time, effort, and expertise required to achieve reasonable protein coverage and reliable quantification have limited the broad application of this technology. To fully leverage mass spectrometry for the elucidation of biological systems requires sufficient throughput to monitor dynamic changes across conditions and to enable replicate analysis to provide statistical power. We report a straightforward approach to increase the multiplexing capacity of quantitative mass spectrometry, which provides a platform for the analysis of cellular signaling pathways. Using triplex metabolic labeling and six-plex isobaric tags, we monitored changes in protein abundance from 18 samples simultaneously, performing biological triplicates of a six-point time course of rapamycin-stimulated yeast. The data set provides temporal abundance profiles for thousands of yeast proteins, highlighting the complex cellular roles of the TOR (target of rapamycin) pathway.

* To whom correspondence should be addressed. E-mail: sgygi{at}hms.harvard.edu

Citation: N. Dephoure, S. P. Gygi, Hyperplexing: A Method for Higher-Order Multiplexed Quantitative Proteomics Provides a Map of the Dynamic Response to Rapamycin in Yeast. Sci. Signal. 5, rs2 (2012).

Read the Full Text

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Latency-Associated Degradation of the MRP1 Drug Transporter During Latent Human Cytomegalovirus Infection.
M. P. Weekes, S. Y. L. Tan, E. Poole, S. Talbot, R. Antrobus, D. L. Smith, C. Montag, S. P. Gygi, J. H. Sinclair, and P. J. Lehner (2013)
Science 340, 199-202
   Abstract »    Full Text »    PDF »
Protein Complex-Based Analysis Framework for High-Throughput Data Sets.
A. Vinayagam, Y. Hu, M. Kulkarni, C. Roesel, R. Sopko, S. E. Mohr, and N. Perrimon (2013)
Science Signaling 6, rs5
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882