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TitleNucleoside diphosphate kinase A (NME1) catalyses its own oligophosphorylation.
Journal, issue, pagesNat Chem, Vol. 17, Issue 11, Page 1757-1767, Year 2025
Publish dateAug 20, 2025
AuthorsArif Celik / Felix Schöpf / Christian E Stieger / Sarah Lampe / Björn Hanf / Jeremy A M Morgan / Max Ruwolt / Fan Liu / Christian P R Hackenberger / Daniel Roderer / Dorothea Fiedler /
PubMed AbstractProtein phosphorylation is a central signalling mechanism in eukaryotic cells. The scope of this post-translational modification includes protein pyro- and polyphosphorylation. Here we report the ...Protein phosphorylation is a central signalling mechanism in eukaryotic cells. The scope of this post-translational modification includes protein pyro- and polyphosphorylation. Here we report the discovery of another mode of phosphorylation: protein oligophosphorylation. Using site-specifically phosphorylated and pyrophosphorylated nucleoside diphosphate kinase A (NME1), the effects of these modifications on enzyme activity were investigated. Phosphorylation, and more so pyrophosphorylation, on Thr94 reduced the nucleoside diphosphate kinase activity. Nevertheless, both phosphoprotein and pyrophosphoprotein catalysed their own oligophosphorylation-up to the formation of a hexaphosphate chain-using ATP as a cofactor. Oligophosphorylation was critically dependent on the catalytic histidine residue His118, and cryogenic electron microscopy analysis of the modified proteins suggests an intramolecular phosphoryl transfer mechanism. Oligophosphorylation of NME1 in biochemical samples, and in cell lysates, was further confirmed using mass spectrometry, and was found to promote a new set of protein interactions. Our results highlight the complex nature of phosphoregulation, and the methods described here provide the opportunity to investigate the impact of this unusual modification in the future.
External linksNat Chem / PubMed:40835738 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.8 Å
Structure data

51248

9gd6

EMDB-51248, PDB-9gd6:
NME1 94-Phosphoserine
Method: EM (single particle) / Resolution: 2.8 Å

51250

9gd8

EMDB-51250, PDB-9gd8:
NME1 94-Diphosphoserine
Method: EM (single particle) / Resolution: 3.3 Å

51251

9gd9

EMDB-51251, PDB-9gd9:
NME1 94-Oligophosphoserine
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / nucleotide kinase / post-translational modification / phosphorylation

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