Ubiquitin and ubiquitin-like proteins (UBLs) are essential regulators of a multitude of cellular processes, including autophagy. It is known that these proteins relay their effects by covalently modifying their substrate molecules. As an exception to this norm, Pang et al. report a novel phenomenon in which the UBL ATG12 interacts with its substrate ATG5 in a non-covalent fashion to promote autophagy in apicomplexan parasites and some yeasts.
This is a preview of subscription content, log in via an institution to check access.
References
Dikic, I. Annu. Rev. Biochem. 86, 193–224 (2017).
Fujioka, Y. et al. J. Biol. Chem. 283, 1921–1928 (2008).
Hanada, T. et al. J. Biol. Chem. 282, 37298–37302 (2007).
Mizushima, N. et al. Nature 395, 395–398 (1998).
Mizushima, N. et al. Nat. Struct. Molec. Biol. https://doi.org/10.1038/s41594-019-0204-3 (2019).
Mizushima, N., Yoshimori, T. & Ohsumi, Y. FEBS Lett. 532, 1873–3468 (2002).
Mizushima, N. et al. J. Cell Biol. 152, 657–668 (2001).
Suzuki, K. et al. EMBO J. 20, 5971–5981 (2001).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Rights and permissions
About this article
Cite this article
Tiku, V., Dikic, I. Autophagy without conjugation. Nat Struct Mol Biol 26, 249–250 (2019). https://doi.org/10.1038/s41594-019-0207-0
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41594-019-0207-0
- Springer Nature America, Inc.