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The biological impact of mass-spectrometry-based proteomics

Nature volume 450, pages 991–1000 (2007)Cite this article

Abstract

In the past decade, there have been remarkable advances in proteomic technologies. Mass spectrometry has emerged as the preferred method for in-depth characterization of the protein components of biological systems. Using mass spectrometry, key insights into the composition, regulation and function of molecular complexes and pathways have been gained. From these studies, it is clear that mass-spectrometry-based proteomics is now a powerful 'hypothesis-generating engine' that, when combined with complementary molecular, cellular and pharmacological techniques, provides a framework for translating large data sets into an understanding of complex biological processes.

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Figure 1: Discovery of a BAD-containing protein complex that localizes to mitochondria and integrates apoptotic and glycolytic processes.
Figure 2: Discovery of Tfb5 as the tenth subunit of TFIIH, which is involved in transcriptional and DNA-repair processes.
Figure 3: Discovery of chaperone complexes that regulate CFTR folding and endoplasmic-reticulum-mediated export.
Figure 4: Identification of male-gametocyte-specific and female-gametocyte-specific proteins in Plasmodium berghei.
Figure 5: Discovery of an ether-lipid signalling pathway that supports cancer pathogenesis.
Figure 6: Identification of candidate ATM and/or ATR substrates involved in the DNA-damage response.
Figure 7: Discovery of DAF-2-regulated protein pathways that modulate longevity in Caenorhabditis elegans.

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Acknowledgements

We gratefully acknowledge the support of the National Institutes of Health.

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Authors and Affiliations

  1. Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 92037, California, USA

    Benjamin F. Cravatt, Gabriel M. Simon & John R. Yates III

  2. The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 92037, California, USA

    Benjamin F. Cravatt & Gabriel M. Simon

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Correspondence should be addressed to B.F.C. (cravatt@scripps.edu) or J.R.Y. (jyates@scripps.edu).

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Cravatt, B., Simon, G. & Yates III, J. The biological impact of mass-spectrometry-based proteomics. Nature 450, 991–1000 (2007). https://doi.org/10.1038/nature06525

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