Accession PRJCA027542
Title Nuclear dihydroxyacetone phosphate signals nutrient sufficiency and cell cycle phase to global histone acetylation
Relevance Metabolism
Data types Transcriptome or Gene expression
LC-MS data
Organisms Homo sapiens
Description Global histone acetylation varies with changes in the nutrient and cell cycle phases; however, the mechanisms connecting these variations are not fully understood. Herein, we report that nutrient-related and cell-cycle-regulated nuclear acetate regulates global histone acetylation. Histone deacetylation-generated acetate accumulates in the nucleus and induces histone hyperacetylation. The nuclear acetate levels were controlled by glycolytic enzyme triosephosphate isomerase 1 (TPI1). Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP. CDK2 accumulates in the cytosol during the late G1/S phases. Inactivation or blockade of nuclear translocation of TPI1 abrogates nutrient-dependent and cell-cycle-dependent global histone acetylation, chromatin condensation, gene transcription and DNA replication. These results identify the mechanism of maintaining global histone acetylation by nutrient and cell cycle signals.
Sample scope Monoisolate
Release date 2024-06-29
Publication
PubMed ID Article title Journal name DOI Year
34140692
Grants
Agency program Grant ID Grant title
Ministry of Science and Technology of the People's Republic of China (MOST) 2018YFA0800300
Ministry of Science and Technology of the People's Republic of China (MOST) 2018YFA0801300
National Natural Science Foundation of China (NSFC) 31821002
Submitter Jiaojiao Zhang (17110700011@fudan.edu.cn)
Organization Fudan University
Submission date 2024-06-29

Project Data

Resource name Description