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 +9 more
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TLDR
The previously uncharacterized NMR properties of lysine propionylation, butyrylation, succinylation, malonylation and crotonylation are delineated to define an initial reference frame for comprehensive PTM studies by high-resolution 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.read more
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Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch
Alaji Bah,Robert M. Vernon,Zeba N. Siddiqui,Mickael Krzeminski,Ranjith Muhandiram,Charlie Zhao,Nahum Sonenberg,Lewis E. Kay,Julie D. Forman-Kay +8 more
TL;DR: Stabilization of a phosphorylation-induced fold is highlighted as the essential mechanism for phospho-regulation of the 4E-BP:eIF4E interaction and exemplify a new mode of biological regulation mediated by intrinsically disordered proteins.
Journal ArticleDOI
Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications
Alaji Bah,Julie D. Forman-Kay +1 more
TL;DR: Diverse biological processes that are dependent on PTM regulation of IDPs are discussed and recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms are presented.
Journal ArticleDOI
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).
Francois Xavier Theillet,Andres Binolfi,Tamara Frembgen-Kesner,Karan S. Hingorani,Mohona Sarkar,Ciara Kyne,Conggang Li,Peter B. Crowley,Lila M. Gierasch,Gary J. Pielak,Adrian H. Elcock,Anne Gershenson,Philipp Selenko +12 more
TL;DR: This work has learned about the unexpected intracellular stability of disordered proteins, their roles in integrating post-translational protein modifications in cell signaling and about their functions in regulatory processes ranging from transcription to cell fate decisions.
Journal ArticleDOI
Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation.
Veronica H Ryan,Gregory L. Dignon,Gül H. Zerze,C.V. Chabata,Rute Silva,Alexander E. Conicella,Joshua Amaya,Kathleen A. Burke,Jeetain Mittal,Nicolas L. Fawzi +9 more
TL;DR: A unified structural view of hnRNPA2 self-assembly, aggregation, and interaction and the distinct effects of small chemical changes-disease mutations and arginine methylation-on these assemblies are provided.
Journal ArticleDOI
Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation
TL;DR: It is shown that the unphosphorylated Ash1 IDR adopts coil-like conformations that are expanded and well-solvated, and this result contradicts inferences regarding global compaction that are derived from heuristics based on amino acid compositions for IDRs with low proline contents.
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