PBS3 通过保护 EDS1 来抵御植物免疫中的蛋白酶体介导的降解。
PBS3 Protects EDS1 from Proteasome-Mediated Degradation in Plant Immunity.
机构信息
Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing 210014, China; Department of Biological Sciences, University of South Carolina, Columbia, SC 29208, USA.
Texas A&M AgriLife Research Center at Dallas, Texas A&M University System, Dallas, TX 75252, USA.
出版信息
Mol Plant. 2019 May 6;12(5):678-688. doi: 10.1016/j.molp.2019.01.023. Epub 2019 Feb 11.
Plant immunity is controlled by both positive regulators such as PBS3 and EDS1 and negative regulators such as NPR3 and NPR4. However, the relationships among these important immune regulators remain elusive. In this study, we found that PBS3 interacts with EDS1 in both the cytoplasm and the nucleus, and is required for EDS1 protein accumulation. NPR3 and NPR4, which function as salicylic acid receptors and adaptors of Cullin3-based E3 ligase, interact with and mediate the degradation of EDS1 via the 26S proteasome. We further discovered that PBS3 inhibits the polyubiquitination and subsequent degradation of EDS1 by reducing the association of EDS1 with the Cullin3 adaptors NPR3 and NPR4. Furthermore, we showed that PBS3 and EDS1 also contribute to PAMP-triggered immunity in addition to effector-triggered immunity. Collectively, our study reveals a novel mechanism by which plants fine-tune defense responses by inhibiting the degradation of a positive player in plant immunity.
植物免疫受到 PBS3 和 EDS1 等正向调节剂以及 NPR3 和 NPR4 等负向调节剂的控制。然而，这些重要免疫调节剂之间的关系仍然难以捉摸。在这项研究中，我们发现 PBS3 在细胞质和细胞核中均与 EDS1 相互作用，并且是 EDS1 蛋白积累所必需的。NPR3 和 NPR4 作为水杨酸受体和 Cullin3 基 E3 连接酶的衔接蛋白，通过 26S 蛋白酶体相互作用并介导 EDS1 的降解。我们进一步发现，PBS3 通过减少 EDS1 与 Cullin3 衔接蛋白 NPR3 和 NPR4 的结合，抑制 EDS1 的多泛素化和随后的降解。此外，我们还表明，PBS3 和 EDS1 除了参与效应物触发的免疫反应外，还参与了 PAMP 触发的免疫反应。总之，我们的研究揭示了一种新的机制，植物通过抑制植物免疫中正向调控因子的降解来精细调控防御反应。
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