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Mapping protein post-translational modifications with mass spectrometry

Nature Methods volume 4, pages 798–806 (2007)Cite this article

Abstract

Post-translational modifications of proteins control many biological processes, and examining their diversity is critical for understanding mechanisms of cell regulation. Mass spectrometry is a fundamental tool for detecting and mapping covalent modifications and quantifying their changes. Modern approaches have made large-scale experiments possible, screening complex mixtures of proteins for alterations in chemical modifications. By profiling protein chemistries, biologists can gain deeper insight into biological control. The aim of this review is introduce biologists to current strategies in mass spectrometry–based proteomics that are used to characterize protein post-translational modifications, noting strengths and shortcomings of various approaches.

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Figure 1: Flow chart for using MS to detect and analyze protein post-translational modifications described in this review.
Figure 2: Common methods used for phosphopeptide quantification.
Figure 3: Determining stoichiometry of phosphorylation.

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Acknowledgements

We gratefully acknowledge support from US National Institutes of Health grants CA112847 (E.S.W.), CA126240 (K.A.R.) and CA118972 (N.G.A.).

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  1. Eric S Witze and William M Old: These authors contributed equally to this work.

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  1. Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, 80309-0215, Colorado, USA

    Eric S Witze, William M Old, Katheryn A Resing & Natalie G Ahn

  2. Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, 80309-0215, Colorado, USA

    Natalie G Ahn

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Witze, E., Old, W., Resing, K. et al. Mapping protein post-translational modifications with mass spectrometry. Nat Methods 4, 798–806 (2007). https://doi.org/10.1038/nmeth1100

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