Plant E3 ligases: Flexible enzymes in a sessile world

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Abstract

Since its discovery in the late 1970s, the ubiquitin proteasome pathway appears to be omnipresent in many research fields. Although originally discovered in animals, the pathway has a very central role in plants, which may be correlated to their sessile lifestyle. E3 ligases function as flexible and highly diverse key regulators within the pathway by targeting substrate proteins for ubiquitylation, and often proteolytic degradation via the 26S proteasome. This review provides a concise overview on the most common classes of E3 ligases so far described in plants, and emphasizes recent findings regarding these interesting and flexible enzymes and their diverse functions in plant biology. © 2013 © The Author 2013. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPB and IPPE, SIBS, CAS.

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Chen, L., & Hellmann, H. (2013). Plant E3 ligases: Flexible enzymes in a sessile world. Molecular Plant. Oxford University Press. https://doi.org/10.1093/mp/sst005

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