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Functional and quantitative proteomics using SILAC

Nature Reviews Molecular Cell Biology volume 7, pages 952–958 (2006)Cite this article

Abstract

Researchers in many biological areas now routinely characterize proteins by mass spectrometry. Among the many formats for quantitative proteomics, stable-isotope labelling by amino acids in cell culture (SILAC) has emerged as a simple and powerful one. SILAC removes false positives in protein-interaction studies, reveals large-scale kinetics of proteomes and — as a quantitative phosphoproteomics technology — directly uncovers important points in the signalling pathways that control cellular decisions.

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Figure 1: Interaction of a bacterial phosphoprotein with a human host protein.
Figure 2: Systems biology of stem-cell differentiation.
Figure 3: Nucleolar proteome dynamics.

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Acknowledgements

I thank S.-E. Ong, L. Foster, B. Blagoev, J. Andersen and members of the Department for Proteomics and Signal Transduction for critical discussion of this manuscript. This work was supported by the Danish National Research Foundation and the Max-Planck Society.

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  1. the Department of Proteomics and Signal Transduction, Max-Planck Institute for Biochemistry, Am Klopferspitz 18, Martinsried, D-82152, Germany

    Matthias Mann

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DATABASES

Matthias Mann 's homepage

Pandey laboratory SILAC pages at John Hopkins University

Open source program MSQuant, which allows quantitation of SILAC data

Phosphorylation sites database (Phosida) at the Max-Planck-Institut for Biochemistry

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Mann, M. Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7, 952–958 (2006). https://doi.org/10.1038/nrm2067

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