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Cell signaling, post-translational protein modifications and NMR spectroscopy

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A Protocol for this article was published on 27 June 2013

Abstract

Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical environments of individual protein residues, which are readily detected by high-resolution NMR spectroscopy. In the following, we provide a concise compendium of NMR characteristics of the main types of eukaryotic PTMs: serine, threonine, tyrosine and histidine phosphorylation, lysine acetylation, lysine and arginine methylation, and serine, threonine O-glycosylation. We further delineate the previously uncharacterized NMR properties of lysine propionylation, butyrylation, succinylation, malonylation and crotonylation, which, altogether, define an initial reference frame for comprehensive PTM studies by high-resolution NMR spectroscopy.

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Acknowledgments

We would like to thank Rachel Klevit, Olga Vinogradova, Tanja Mittag and Julie Forman-Kay for providing original NMR spectra for reproduction in this manuscript. F.X.T. acknowledges support from the Association pour la Researche contre le Cancer (ARC). P.S. acknowledges funding by an Emmy Noether research grant (SE1794/1-1) from the Deutsche Forschungsgemeinschaft (DFG). R. W. K. acknowledges support from NIH core grant P30CA21765 (to St. Jude Children’s Research Hospital) and 5R01CA082491 (to R. W. K.), and the American Lebanese Syrian Associated Charities (ALSAC) of St. Jude Children’s Research Hospital. We further express our gratitude to Angela Gronenborn and Georges Mer for expert advice and stimulating discussions in the course of writing the paper.

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  1. Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125, Berlin, Germany

    Francois-Xavier Theillet, Stamatios Liokatis, Rossukon Thongwichian, Jonas Kosten & Philipp Selenko

  2. CNRS UMR 8576, Universite Lille Nord de France, 59655, Villeneuve d’Ascq, France

    Caroline Smet-Nocca, Isabelle Landrieu & Guy Lippens

  3. Department of Structural Biology, St. Jude Children’s Research Hospital, Memphis, TN, USA

    Mi-Kyung Yoon & Richard W. Kriwacki

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Theillet, FX., Smet-Nocca, C., Liokatis, S. et al. Cell signaling, post-translational protein modifications and NMR spectroscopy. J Biomol NMR 54, 217–236 (2012). https://doi.org/10.1007/s10858-012-9674-x

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