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. 2015 Feb 13;15:49. doi: 10.1186/s12870-015-0442-4

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© Wang et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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A proposed model for OsPUB15 to regulate PID2-mediated signaling. The unknown ligand from pathogen is likely able to activate the immune receptor PID2 by changing its conformation, which leads directly to the homodimerization and autophosphorylation of PID2. Such phosphorylated form of PID2 then recruits and transphosphorylates OsPUB15. The phosphorylated OsPUB15 serves as an active E3 ligase to mediate the degradation of unknown substrate(s), which is/are likely involved in PID2-mediated immune responses.