Under steady-state conditions, the E3 ubiquitin ligase Parkin is localized to the cytosol in an autoinhibited state. Two recent studies describe the mechanism of Parkin activation by phosphorylation via structural rearrangement of the Ubl and RING2 domains, explaining how the RING2 domain is released from the core of Parkin to allow for ubiquitination of its substrates.
References
Kalia, L. V. & Lang, A. E. Lancet 386, 896–912 (2015).
Kitada, T. et al. Nature 392, 605–608 (1998).
Valente, E. M. et al. Science 304, 1158–1160 (2004).
Seirafi, M., Kozlov, G. & Gehring, K. FEBS J. 282, 2076–2088 (2015).
Narendra, D. P. et al. PLoS Biol. 8, e1000298 (2010).
Shiba-Fukushima, K. et al. PLoS Genet. 10, e1004861 (2014).
Kazlauskaite, A. et al. EMBO Rep. 16, 939–954 (2015).
Kane, L. A. et al. J. Cell Biol. 205, 143–153 (2014).
Kazlauskaite, A. et al. Biochem. J. 460, 127–139 (2014).
Koyano, F. et al. Nature 510, 162–166 (2014).
Ordureau, A. et al. Mol. Cell 56, 360–375 (2014).
Wauer, T., Simicek, M., Schubert, A. & Komander, D. Nature 524, 370–374 (2015).
Trempe, J. F. et al. Science 340, 1451–1455 (2013).
Kumar, A. et al. Nat. Struct. Mol. Biol. 24, 475–483 (2017).
Sauvé, V. et al. Nat. Struct. Mol. Biol. 25, 623–630 (2018).
Gladkova, C., Maslen, S. L., Skehel, J. M. & Komander, D. Nature 559, 410–414 (2018).
Sarraf, S. A. et al. Nature 496, 372–376 (2013).
Ordureau, A. et al. Mol. Cell 70, 211–227 (2018).
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Le Guerroué, F., Youle, R.J. Active state of Parkin. Nat Struct Mol Biol 25, 644–646 (2018). https://doi.org/10.1038/s41594-018-0101-1
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DOI: https://doi.org/10.1038/s41594-018-0101-1
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