Small Molecule-Activated O-GlcNAcase for Spatiotemporal Removal of O-GlcNAc in Live Cells

ACS Chem Biol. 2023 Jan 20;18(1):193-201. doi: 10.1021/acschembio.2c00894. Epub 2023 Jan 4.

Abstract

The nutrient sensor O-linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification found on thousands of nucleocytoplasmic proteins. O-GlcNAc levels in cells dynamically respond to environmental cues in a temporal and spatial manner, leading to altered signal transduction and functional effects. The spatiotemporal regulation of O-GlcNAc levels would accelerate functional interrogation of O-GlcNAc and manipulation of cell behaviors for desired outcomes. Here, we report a strategy for spatiotemporal reduction of O-GlcNAc in live cells by designing an O-GlcNAcase (OGA) fused to an intein triggered by 4-hydroxytamoxifen (4-HT). After rational protein engineering and optimization, we identified an OGA-intein variant whose deglycosidase activity can be triggered in the desired subcellular compartments by 4-HT in a time- and dose-dependent manner. Finally, we demonstrated that 4-HT activation of the OGA-intein fusion can likewise potentiate inhibitory effects in breast cancer cells by virtue of the reduction of O-GlcNAc. The spatiotemporal control of O-GlcNAc through the chemically activatable OGA-intein fusion will facilitate the manipulation and functional understanding of O-GlcNAc in live cells.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetylglucosamine* / metabolism
  • N-Acetylglucosaminyltransferases / genetics
  • Protein Processing, Post-Translational
  • Signal Transduction
  • beta-N-Acetylhexosaminidases* / genetics

Substances

  • hexosaminidase C
  • Acetylglucosamine
  • beta-N-Acetylhexosaminidases
  • N-Acetylglucosaminyltransferases