Journal
PLANT PHYSIOLOGY
Volume 183, Issue 3, Pages 1364-1375Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.19.01265
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Funding
- National Institutes of Health National Institute of General Medical Sciences [R01GM121445]
- Next-Generation BioGreen 21 Program Systems and Synthetic Agrobiotech Center, Rural Development Administration, Republic of Korea [PJ013254, PJ01116604]
- Third Call of the European Research Area Net for Coordinating Action in Plant Sciences
- National Science Foundation [1826803]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1826803] Funding Source: National Science Foundation
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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 (Arabidopsis thaliana) 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 Arabidopsisp2k1mutant. 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 [K-d] = 44.47 +/- 15.73 nm). Interestingly,p2k2andp2k1 p2k2mutant plants showed increased susceptibility to the pathogenPseudomonas syringae,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. A receptor kinase that can bind to ATP with high affinity plays a partially redundant role during plant immunity.
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