title: Cell signaling, post-translational protein modifications and NMR spectroscopy.
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.
authors.affiliation: Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), In-cell NMR Group, Robert-Roessle Strasse 10, 13125 Berlin, Germany.
authors.forename: Francois-Xavier
authors.initials: FX
authors.lastname: Theillet
authors.forename: Caroline
authors.initials: C
authors.lastname: Smet-Nocca
authors.forename: Stamatios
authors.initials: S
authors.lastname: Liokatis
authors.forename: Rossukon
authors.initials: R
authors.lastname: Thongwichian
authors.forename: Jonas
authors.initials: J
authors.lastname: Kosten
authors.forename: Mi-Kyung
authors.initials: MK
authors.lastname: Yoon
authors.forename: Richard W
authors.initials: RW
authors.lastname: Kriwacki
authors.forename: Isabelle
authors.initials: I
authors.lastname: Landrieu
authors.forename: Guy
authors.initials: G
authors.lastname: Lippens
authors.forename: Philipp
authors.initials: P
authors.lastname: Selenko
mesh_terms: D000107:Acetylation; D000215:Acylation; D000478:Alkylation; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D001120:Arginine / Q000378:metabolism; D002450:Cell Communication; D005057:Eukaryotic Cells / Q000378:metabolism; D006031:Glycosylation; D006639:Histidine / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008745:Methylation; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D013912:Threonine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
chemical_list: D000596:Amino Acids; D011506:Proteins; D013912:Threonine; D014443:Tyrosine; D012694:Serine; D006639:Histidine; D001120:Arginine; D008239:Lysine