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Spatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT

Nature Chemical Biology volume 21, pages 300–308 (2025)Cite this article

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Abstract

The post-translational modification of intracellular proteins through O-linked β-N-acetylglucosamine (O-GlcNAc) is a conserved regulatory mechanism in multicellular organisms. Catalyzed by O-GlcNAc transferase (OGT), this dynamic modification has an essential role in signal transduction, gene expression, organelle function and systemic physiology. Here, we present Opto-OGT, an optogenetic probe that allows for precise spatiotemporal control of OGT activity through light stimulation. By fusing a photosensitive cryptochrome protein to OGT, Opto-OGT can be robustly and reversibly activated with high temporal resolution by blue light and exhibits minimal background activity without illumination. Transient activation of Opto-OGT results in mTORC activation and AMPK suppression, which recapitulate nutrient-sensing signaling. Furthermore, Opto-OGT can be customized to localize to specific subcellular sites. By targeting OGT to the plasma membrane, we demonstrate the downregulation of site-specific AKT phosphorylation and signaling outputs in response to insulin stimulation. Thus, Opto-OGT is a powerful tool for defining the role of O-GlcNAcylation in cell signaling and physiology.

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Fig. 1: Design and characterization of Opto-OGT.
Fig. 2: Opto-OGT is tunable and reversible, and further characterization of Opto-OGT reveals the requirements for it to work.
Fig. 3: Optogenetic activation of OGT reveals temporal dependence of nutrient status sensing.
Fig. 4: Optogenetic activation of OGT via CIBN−CRY2 recruitment results in a subcellular compartment-specific increase of O-GlcNAcylation.

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Data availability

The MS proteomics data have been deposited to the JPOST repository with the dataset identifier JPST002053. Further information on the MS data and AlphaFold simulation is available in the Supplementary Information. Data supporting the findings of this study are available in the Article, Supplementary Videos and Supplementary Information. Source data are provided with this paper.

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Acknowledgements

This work was supported by the National Institutes of Health (R01DK089098, R01DK137467 and R01DK102648 to X.Y.), American Diabetes Association (1-19-IBS-119 to X.Y.), intramural support from the Agency for Science, Technology and Research (A*STAR) Biomedical Research Council core fund (to W.H.), A*STAR Strategic Research Program (the Brain-Body Initiative, iGrants no. 21718 to W.H.), an A*STAR Use-Inspired Basic Research award (to W.H.), the National Research Foundation Competitive Research Program (NRF-CRP23-2019-0004 to W.H.) and the National Medical Research Council Young Individual Research Grant (OFYIRG19nov-0045 to Q.O.). We thank P. L. Chia and H. Mao for proofreading the manuscript.

Author information

Authors and Affiliations

  1. Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore

    Qunxiang Ong, Ler Ting Rachel Lim, Cameron Goh, Sher En Chan, Crystal Jing Yi Lim, Valerie Kam, Jerome Yap, Siew Lan Lim, Sun-Yee Kim & Weiping Han

  2. Department of Comparative Medicine, Yale University School of Medicine, New Haven, CT, USA

    Qunxiang Ong, Tiffany Tseng, Reina Desrouleaux, Anton M. Bennett & Xiaoyong Yang

  3. Duke-NUS Medical School, National University of Singapore, Singapore, Singapore

    Yilie Liao

  4. Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT, USA

    Tiffany Tseng, Reina Desrouleaux & Xiaoyong Yang

  5. Functional Proteomics Laboratory, SingMass National Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore

    Loo Chien Wang, Siok Ghee Ler & Radoslaw M. Sobota

  6. Yale Center for Molecular and Systems Metabolism, Yale University School of Medicine, New Haven, CT, USA

    Anton M. Bennett & Xiaoyong Yang

  7. Department of Pharmacology, Yale University School of Medicine, New Haven, CT, USA

    Anton M. Bennett

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  1. Qunxiang Ong
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Contributions

Q.O., W.H. and X.Y. conceived the project. Q.O., Y.L. and X.Y. designed the experiments. Q.O., L.T.R.L., S.E.C., C.J.Y.L., V.K., J.Y. and T.T. performed the optogenetic experiments. Q.O., S.E.C., C.J.Y.L., S.-Y.K. and S.L.L. performed cloning experiments. Q.O. and C.G. performed the AlphaFold experiments. L.C.W and S.G.L. performed the MS experiments. Q.O., C.G., Y.L., V.K., T.T., L.C.W and S.G.L. analyzed the data. L.T.R.L., S.E.C., R.D., A.B. and R.S. offered technical advice. Q.O., A.B., W.H. and X.Y. wrote the paper with input from all authors.

Corresponding authors

Correspondence to Weiping Han or Xiaoyong Yang.

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Nature Chemical Biology thanks Luc Bertrand, Robert Hughes and the other, anonymous, reviewer(s) for their contribution to the peer review of this work.

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Extended data

Extended Data Fig. 1 Comparison of nutrient sensing pathways when subjected to glucose concentration changes or Opto-OGT activation.

a, Representative Western blots of key nutrient sensing pathways when HEK293T cells are subjected to glucose concentration changes from 0 mM to 25 mM. Immunoblots shown are representative of two independent biological repeats. b, Representative Western blots of HEK293T cells transfected with OGT-mCherry-CRY2 undergoing 15 minutes of blue light. Key downstream signaling pathways are probed as labelled. Immunoblots shown are representative of two independent biological repeats. c, Representative Western blots of phosphor-ULK1 when HEK293T cells transfected with OGT-mCherry-CRY2 underwent 15 minutes of blue light. Immunoblots shown are representative of two independent biological repeats.

Source data

Supplementary information

Supplementary Information

Supplementary Tables 1 and 2, Figs. 1–11 and source data for supplementary figures.

Reporting Summary

Supplementary Video 1

Movie showing HEK293T cells transfected with OGT−mCherry−CRY2. The first 300 s are without blue light, while in the next 300 s, the cells are supplied with blue light at a 100-ms pulse every 5 s. No blue light is illuminated from 600−1,800 s and blue light is reapplied from 1,800−2,400 s at a 100-ms pulse every 5 s.

Supplementary Video 2

Movie showing COS-7 cells transfected with both OGT−mCherry−CRY2 (right) and CIBN−GFP−miro (left). Green and blue lights are continually supplied to the system at a 100-ms pulse every 15 s.

Supplementary Video 3

Movie showing HEK293T cells transfected with both OGT−mCherry−CRY2 (right) and CIBN−GFP−CAAX (left). Green and blue lights are continually supplied to the system at a 100-ms pulse every 5 s.

Source data

Source Data Fig. 1

Statistical source data.

Source Data Fig. 1

Unprocessed western blots and MS statistical source data.

Source Data Fig. 2

Statistical source data

Source Data Fig. 2

Unprocessed western blots.

Source Data Fig. 3

Statistical source data.

Source Data Fig. 4

Statistical source data.

Source Data Fig. 4

Unprocessed western blots.

Source Data Extended Data Fig. 1

Unprocessed western blots.

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Ong, Q., Lim, L.T.R., Goh, C. et al. Spatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT. Nat Chem Biol 21, 300–308 (2025). https://doi.org/10.1038/s41589-024-01770-7

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