Abstract
The ubiquitin-proteasome system (UPS) controls intracellular protein degradation in all eukaryotic cells and provides a powerful and versatile mechanism through which the activity of specific proteins can be temporally downregulated. In this system, a trio of enzymes known as E1, E2, and E3 promotes the posttranslational modification of protein substrates with a polyubiquitin chain, which serves as the signal for proteasome-mediated proteolysis. In response to various cellular cues, the E3 ubiquitin ligases act at the end of the three-enzyme cascade and play a critical role in both recognizing specific protein targets and facilitating ubiquitin transfer from the E2 enzyme to the substrate. By coupling hormone perception with substrate recognition through the E3 ligases, plants have evolved elegant strategies to use UPS-mediated protein degradation as a primary means to relay hormonal signals. In the plant genomes, the large number of UPS components, particularly the cullin-RING E3 complexes, suggests that the extent of cellular regulation by protein degradation far exceeds what has been realized to date.
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Acknowledgments
D. V. R. and N. Z. are supported by Howard Hughes Medical Institute. Published studies from the Zheng laboratory related to the topics discussed in this chapter have been sponsored by Howard Hughes Medical Institute, National Institutes of Health, National Science Foundation, The Pew Charitable Trusts, Burroughs Wellcome Fund, and the University of Washington, Seattle, WA, USA.
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Rusnac, D.V., Zheng, N. (2018). Overview of Protein Degradation in Plant Hormone Signaling. In: Hejátko, J., Hakoshima, T. (eds) Plant Structural Biology: Hormonal Regulations. Springer, Cham. https://doi.org/10.1007/978-3-319-91352-0_2
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