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.
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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).
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Tiku, V., Dikic, I. Autophagy without conjugation. Nat Struct Mol Biol 26, 249–250 (2019). https://doi.org/10.1038/s41594-019-0207-0