Divisions of Plant Science and Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, Missouri 65211.
Cuu Long Delta Rice Research Institute, Cantho 00000, Vietnam.
Plant Physiol. 2020 Jul;183(3):1364-1375. doi: 10.1104/pp.19.01265. Epub 2020 Apr 28.
In animals, extracellular ATP is a well-studied signaling molecule that is recognized by plasma membrane-localized P2-type purinergic receptors. However, in contrast, much less is known about purinergic signaling in plants. P2 receptors play critical roles in a variety of animal biological processes, including immune system regulation. The first plant purinergic receptor, Arabidopsis () P2K1 (L-type lectin receptor kinase-I.9), was shown to contribute to plant defense against bacterial, oomycete, and fungal pathogens. Here, we demonstrate the isolation of a second purinergic receptor, P2K2, by complementation of an Arabidopsis mutant. P2K2 (LecRK-I.5) has 74% amino acid similarity to P2K1. The P2K2 extracellular lectin domain binds to ATP with higher affinity than P2K1 (dissociation constant [ ] = 44.47 ± 15.73 nm). Interestingly, and mutant plants showed increased susceptibility to the pathogen with the double mutant showing a stronger phenotype. In vitro and in planta studies demonstrate that P2K2 and P2K1 interact and cross-phosphorylate upon extracellular ATP treatment. Thus, similar to animals, plants possess multiple purinergic receptors.
在动物中,细胞外 ATP 是一种研究得很好的信号分子,它被质膜定位的 P2 型嘌呤能受体识别。然而,相比之下,人们对植物中的嘌呤能信号知之甚少。P2 受体在包括免疫系统调节在内的多种动物生物学过程中发挥着关键作用。第一个植物嘌呤能受体,拟南芥()P2K1(L 型凝集素受体激酶-I.9),被证明有助于植物抵抗细菌、卵菌和真菌病原体。在这里,我们通过拟南芥()突变体的互补,分离出第二个嘌呤能受体 P2K2。P2K2(LecRK-I.5)与 P2K1 有 74%的氨基酸相似性。P2K2 的细胞外凝集素结构域与 ATP 的结合亲和力高于 P2K1(解离常数 [ ] = 44.47 ± 15.73nm)。有趣的是,和 突变体植物对病原体表现出更高的敏感性,而双突变体表现出更强的表型。体外和体内研究表明,P2K2 和 P2K1 在细胞外 ATP 处理时相互作用并交叉磷酸化。因此,与动物相似,植物具有多种嘌呤能受体。