Regulation of o‐linked n‐acetyl glucosamine transferase (Ogt) through e6 stimulation of the ubiquitin ligase activity of e6ap

Kangli Peng, Ruochuan Liu, Caiwei Jia, Yiyang Wang, Geon H. Jeong, Li Zhou, Ronggui Hu, Hiroaki Kiyokawa, Jun Yin*, Bo Zhao

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Glycosyltransferase OGT catalyzes the conjugation of O‐linked β‐D‐N‐acetylglucosamine (O‐GlcNAc) to Ser and Thr residues of the cellular proteins and regulates many key processes in the cell. Here, we report the identification of OGT as a ubiquitination target of HECT‐type E3 ubiquitin (UB) ligase E6AP, whose overexpression in HEK293 cells would induce the degradation of OGT. We also found that the expression of E6AP in HeLa cells with the endogenous expression of the E6 protein of the human papillomavirus (HPV) would accelerate OGT degradation by the proteasome and suppress O‐GlcNAc modification of OGT substrates in the cell. Overall, our study establishes a new mechanism of OGT regulation by the ubiquitin–proteasome system (UPS) that mediates the crosstalk between protein ubiquitination and O‐GlcNAcylation pathways underlying diverse cellular processes.

Original languageEnglish (US)
Article number10286
JournalInternational journal of molecular sciences
Volume22
Issue number19
DOIs
StatePublished - Oct 1 2021

Keywords

  • E6
  • E6AP
  • Human papillomavirus
  • OGT
  • O‐GlcNAc
  • O‐GlcNAcylation
  • Ubiquitin
  • Ubiquitination

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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