{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["You D"],"funding":["National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["3825"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11076491"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["c-di-AMP is an essential and widespread nucleotide second messenger in bacterial signaling. For most c-di-AMP synthesizing organisms, c-di-AMP homeostasis and the molecular mechanisms pertaining to its signal transduction are of great concern. Here we show that c-di-AMP binds the N-acetylglucosamine (GlcNAc)-sensing regulator DasR, indicating a direct link between c-di-AMP and GlcNAc signaling. Beyond its foundational role in cell-surface structure, GlcNAc is attractive as a major nutrient and messenger molecule regulating multiple cellular processes from bacteria to humans. We show that increased c-di-AMP levels allosterically activate DasR as a master repressor of GlcNAc utilization, causing the shutdown of the DasR-mediated GlcNAc signaling cascade and leading to a consistent enhancemen"],"journal":["Nature communications"],"pubmed_title":["Allosteric regulation by c-di-AMP modulates a complete N-acetylglucosamine signaling cascade in Saccharopolyspora erythraea."],"pmcid":["PMC11076491"],"funding_grant_id":["32070066"],"pubmed_authors":["Ye BC","Chen ZQ","Peng ZY","You D","Zhao LC","Fu Y"],"additional_accession":[]},"is_claimable":false,"name":"Allosteric regulation by c-di-AMP modulates a complete N-acetylglucosamine signaling cascade in Saccharopolyspora erythraea.","description":"c-di-AMP is an essential and widespread nucleotide second messenger in bacterial signaling. For most c-di-AMP synthesizing organisms, c-di-AMP homeostasis and the molecular mechanisms pertaining to its signal transduction are of great concern. Here we show that c-di-AMP binds the N-acetylglucosamine (GlcNAc)-sensing regulator DasR, indicating a direct link between c-di-AMP and GlcNAc signaling. Beyond its foundational role in cell-surface structure, GlcNAc is attractive as a major nutrient and messenger molecule regulating multiple cellular processes from bacteria to humans. We show that increased c-di-AMP levels allosterically activate DasR as a master repressor of GlcNAc utilization, causing the shutdown of the DasR-mediated GlcNAc signaling cascade and leading to a consistent enhancemen","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T21:23:39.277Z","creation":"2026-04-20T03:14:22.098Z"},"accession":"S-EPMC11076491","cross_references":{"pubmed":["38714645"],"doi":["10.1038/s41467-024-48063-0"]}}