An Uncommon Phosphorylation Mode Regulates the Activity and Protein Interactions of <i>N</i>-Acetylglucosamine Kinase.

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 N-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

SUBMITTER: Celik A 

PROVIDER: S-EPMC11140747 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature