{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Celik A"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["14807-14815"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11140747"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146(21)"],"pubmed_abstract":["While the function of protein phosphorylation in eukaryotic cell signaling is well established, the role of a closely related modification, protein pyrophosphorylation, is just starting to surface. A recent study has identified several targets of endogenous protein pyrophosphorylation in mammalian cell lines, including <i>N</i>-acetylglucosamine kinase (NAGK). Here, a detailed functional analysis of NAGK phosphorylation and pyrophosphorylation on serine 76 (S76) has been conducted. This analysis was enabled by using amber codon suppression to obtain phosphorylated pS76-NAGK, which was subsequently converted to site-specifically pyrophosphorylated NAGK (ppS76-NAGK) with a phosphorimidazolide reagent. A significant reduction in GlcNAc kinase activity was observed upon phosphorylation and nea"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["An Uncommon Phosphorylation Mode Regulates the Activity and Protein Interactions of &lt;i&gt;N&lt;/i&gt;-Acetylglucosamine Kinase."],"pmcid":["PMC11140747"],"funding_grant_id":["469186007"],"pubmed_authors":["Beyer I","Celik A","Fiedler D"],"additional_accession":[]},"is_claimable":false,"name":"An Uncommon Phosphorylation Mode Regulates the Activity and Protein Interactions of &lt;i&gt;N&lt;/i&gt;-Acetylglucosamine Kinase.","description":"While the function of protein phosphorylation in eukaryotic cell signaling is well established, the role of a closely related modification, protein pyrophosphorylation, is just starting to surface. A recent study has identified several targets of endogenous protein pyrophosphorylation in mammalian cell lines, including <i>N</i>-acetylglucosamine kinase (NAGK). Here, a detailed functional analysis of NAGK phosphorylation and pyrophosphorylation on serine 76 (S76) has been conducted. This analysis was enabled by using amber codon suppression to obtain phosphorylated pS76-NAGK, which was subsequently converted to site-specifically pyrophosphorylated NAGK (ppS76-NAGK) with a phosphorimidazolide reagent. A significant reduction in GlcNAc kinase activity was observed upon phosphorylation and nea","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-03T06:49:10.979Z","creation":"2026-04-25T03:21:51.862Z"},"accession":"S-EPMC11140747","cross_references":{"pubmed":["38733353"],"doi":["10.1021/jacs.4c03069"]}}