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拟南芥 RNA 聚合酶 II C 端结构域磷酸酶样蛋白 1 靶向丝裂原活化蛋白激酶级联反应以抑制植物免疫。

Arabidopsis RNA polymerase II C-terminal domain phosphatase-like 1 targets mitogen-activated protein kinase cascades to suppress plant immunity.

机构信息

Department of Plant Pathology and the Ministry of Agriculture Key Laboratory of Pest Monitoring and Green Management, China Agricultural University, Beijing, 100193, China.

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.

出版信息

J Integr Plant Biol. 2023 Oct;65(10):2380-2394. doi: 10.1111/jipb.13551. Epub 2023 Sep 17.

Abstract

Mitogen-activated protein kinase (MAPK) cascades play pivotal roles in plant defense against phytopathogens downstream of immune receptor complexes. The amplitude and duration of MAPK activation must be strictly controlled, but the underlying mechanism remains unclear. Here, we identified Arabidopsis CPL1 (C-terminal domain phosphatase-like 1) as a negative regulator of microbe-associated molecular pattern (MAMP)-triggered immunity via a forward-genetic screen. Disruption of CPL1 significantly enhanced plant resistance to Pseudomonas pathogens induced by the bacterial peptide flg22. Furthermore, flg22-induced MPK3/MPK4/MPK6 phosphorylation was dramatically elevated in cpl1 mutants but severely impaired in CPL1 overexpression lines, suggesting that CPL1 might interfere with flg22-induced MAPK activation. Indeed, CPL1 directly interacted with MPK3 and MPK6, as well as the upstream MKK4 and MKK5. A firefly luciferase-based complementation assay indicated that the interaction between MKK4/MKK5 and MPK3/MPK6 was significantly reduced in the presence of CPL1. These results suggest that CPL1 plays a novel regulatory role in suppressing MAMP-induced MAPK cascade activation and MAMP-triggered immunity to bacterial pathogens.

摘要

丝裂原活化蛋白激酶(MAPK)级联反应在植物免疫受体复合物下游对植物病原体的防御中起着关键作用。MAPK 激活的幅度和持续时间必须严格控制,但潜在的机制仍不清楚。在这里,我们通过正向遗传学筛选鉴定出拟南芥 CPL1(C 端结构域磷酸酶样 1)是微生物相关分子模式(MAMP)触发免疫的负调节剂。CPL1 的破坏显著增强了植物对细菌肽 flg22 诱导的假单胞菌病原体的抗性。此外,在 cpl1 突变体中,flg22 诱导的 MPK3/MPK4/MPK6 磷酸化显著升高,但在 CPL1 过表达系中严重受损,表明 CPL1 可能干扰 flg22 诱导的 MAPK 激活。事实上,CPL1 直接与 MPK3 和 MPK6 以及上游的 MKK4 和 MKK5 相互作用。基于萤火虫荧光素酶的互补测定表明,在存在 CPL1 的情况下,MKK4/MKK5 和 MPK3/MPK6 之间的相互作用显著降低。这些结果表明,CPL1 在抑制 MAMP 诱导的 MAPK 级联激活和 MAMP 触发的对细菌病原体的免疫中发挥了新的调节作用。

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