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Ubiquitin in autophagy and non-protein ubiquitination

In addition to its role in proteasomal degradation, ubiquitin has multiple roles in autophagy. It can mark proteins for autophagic degradation and actively drive autophagosome formation. Recent work shows that ubiquitin can also be conjugated to phospholipids and other biomolecules.

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Fig. 1: Ubiquitin in autophagy induction and cargo recognition.
Fig. 2: Ubiquitination of non-protein substrates.

References

  1. Yamamoto, H., Zhang, S. & Mizushima, N. Nat. Rev. Genet. 24, 382–400 (2023).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  2. Lazarou, M. et al. Nature 524, 309–314 (2015).

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

  3. Liu, X. M. et al. Mol. Cell 59, 1035–1042 (2015).

    Article  CAS  PubMed  Google Scholar 

  4. Vargas, J. N. S. et al. Mol. Cell 74, 347–362.e6 (2019).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Ravenhill, B. J. et al. Mol. Cell 74, 320–329.e6 (2019).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  6. Turco, E. et al. Nat. Commun. 12, 5212 (2021).

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

  7. Yamamoto, H. et al. Dev. Cell 38, 86–99 (2016).

    Article  CAS  PubMed  Google Scholar 

  8. Yamano, K. et al. J. Cell Biol. 219, e201912144 (2020).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  9. Hama, Y., Kurikawa, Y., Matsui, T., Mizushima, N. & Yamamoto, H. Preprint at bioRxiv https://doi.org/10.1101/2023.08.18.553817 (2023).

  10. Hooper, K. M. et al. J. Cell Biol. 221, e202105112 (2022).

    Article  PubMed  PubMed Central  Google Scholar 

  11. Sakamaki, J. I. et al. Mol. Cell 82, 3677–3692.e11 (2022).

    Article  CAS  PubMed  Google Scholar 

  12. Sakamaki, J. I. & Mizushima, N. Trends Cell Biol. 33, 991–1003 (2023).

    Article  CAS  PubMed  Google Scholar 

  13. Otten, E. G. et al. Nature 594, 111–116 (2021).

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

  14. Kelsall, I. R. et al. EMBO J. 41, e109700 (2022).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  15. Zhu, K. et al. Sci. Adv. 8, eadd4253 (2022).

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgements

The author thanks J. Sakamaki and H. Yamamoto for their helpful comments. This work was supported by a grant for Exploratory Research for Advanced Technology from the Japan Science and Technology Agency (JPMJER1702) and a Grant-in-Aid for Specially Promoted Research from the Japan Society for the Promotion of Science (22H04919).

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Correspondence to Noboru Mizushima.

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Mizushima, N. Ubiquitin in autophagy and non-protein ubiquitination. Nat Struct Mol Biol 31, 208–209 (2024). https://doi.org/10.1038/s41594-024-01217-6

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