AMPK regulates histone H2B O-GlcNAcylation

Qiuran Xu, Caihong Yang, Yu Du, Yali Chen, Hailong Liu, Min Deng, Haoxing Zhang, Lei Zhang, Tongzheng Liu, Qingguang Liu, Liewei Wang, Zhenkun Lou, Huadong Pei

Research output: Contribution to journalArticle

41 Scopus citations


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 -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.

Original languageEnglish (US)
Pages (from-to)5594-5604
Number of pages11
JournalNucleic acids research
Issue number9
StatePublished - May 2014

ASJC Scopus subject areas

  • Genetics

Fingerprint Dive into the research topics of 'AMPK regulates histone H2B O-GlcNAcylation'. Together they form a unique fingerprint.

  • Cite this

    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, H. (2014). AMPK regulates histone H2B O-GlcNAcylation. Nucleic acids research, 42(9), 5594-5604.