Abstract:
:Histone H2B O-GlcNAcylation is an important post-translational modification of chromatin during gene transcription. However, how this epigenetic modification is regulated remains unclear. Here we found that the energy-sensing adenosine-monophosphate-activated protein kinase (AMPK) could suppress histone H2B O-GlcNAcylation. AMPK directly phosphorylates O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT). Although this phosphorylation does not regulate the enzymatic activity of OGT, it inhibits OGT-chromatin association, histone O-GlcNAcylation and gene transcription. Conversely, OGT also O-GlcNAcylates AMPK and positively regulates AMPK activity, creating a feedback loop. Taken together, these results reveal a crosstalk between the LKB1-AMPK and the hexosamine biosynthesis (HBP)-OGT pathways, which coordinate together for the sensing of nutrient state and regulation of gene transcription.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Xu Q,Yang C,Du Y,Chen Y,Liu H,Deng M,Zhang H,Zhang L,Liu T,Liu Q,Wang L,Lou Z,Pei Hdoi
10.1093/nar/gku236subject
Has Abstractpub_date
2014-05-01 00:00:00pages
5594-604issue
9eissn
0305-1048issn
1362-4962pii
gku236journal_volume
42pub_type
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