Journal of Biomolecular NMR

, Volume 54, Issue 3, pp 217–236 | Cite as

Cell signaling, post-translational protein modifications and NMR spectroscopy

  • Francois-Xavier Theillet
  • Caroline Smet-Nocca
  • Stamatios Liokatis
  • Rossukon Thongwichian
  • Jonas Kosten
  • Mi-Kyung Yoon
  • Richard W. Kriwacki
  • Isabelle Landrieu
  • Guy Lippens
  • Philipp Selenko
Perspective

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.

Keywords

Histones p53 CBP/p300 Sic1 Tau Integrin b3 p21 KID Pyk2 HPr 

Supplementary material

10858_2012_9674_MOESM1_ESM.pdf (391 kb)
Supplementary material 1 (PDF 391 kb)

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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Francois-Xavier Theillet
    • 1
  • Caroline Smet-Nocca
    • 2
  • Stamatios Liokatis
    • 1
  • Rossukon Thongwichian
    • 1
  • Jonas Kosten
    • 1
  • Mi-Kyung Yoon
    • 3
  • Richard W. Kriwacki
    • 3
  • Isabelle Landrieu
    • 2
  • Guy Lippens
    • 2
  • Philipp Selenko
    • 1
  1. 1.Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin)In-cell NMR GroupBerlinGermany
  2. 2.CNRS UMR 8576Universite Lille Nord de FranceVilleneuve d’AscqFrance
  3. 3.Department of Structural BiologySt. Jude Children’s Research HospitalMemphisUSA

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