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Arabidopsis Lectin Receptor Kinase P2K2 Is a Second Plant Receptor for Extracellular ATP and Contributes to Innate Immunity.
- Source :
-
Plant physiology [Plant Physiol] 2020 Jul; Vol. 183 (3), pp. 1364-1375. Date of Electronic Publication: 2020 Apr 28. - Publication Year :
- 2020
-
Abstract
- 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 Arabidopsis p2k1 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 [ K <subscript>d</subscript> ] = 44.47 ± 15.73 nm). Interestingly, p2k2 and p2k1 p2k2 mutant plants showed increased susceptibility to the pathogen Pseudomonas 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.<br /> (© 2020 American Society of Plant Biologists. All Rights Reserved.)
- Subjects :
- Arabidopsis Proteins chemistry
Arabidopsis Proteins genetics
Calcium metabolism
Cell Membrane metabolism
Cytosol metabolism
Disease Resistance
Mutation genetics
Phosphorylation
Plant Diseases immunology
Plant Diseases microbiology
Protein Binding
Protein Domains
Protein Serine-Threonine Kinases chemistry
Protein Serine-Threonine Kinases genetics
Pseudomonas syringae physiology
Signal Transduction
Adenosine Triphosphate metabolism
Arabidopsis enzymology
Arabidopsis immunology
Arabidopsis Proteins metabolism
Extracellular Space metabolism
Immunity, Innate
Lectins metabolism
Plant Immunity
Protein Serine-Threonine Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1532-2548
- Volume :
- 183
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Plant physiology
- Publication Type :
- Academic Journal
- Accession number :
- 32345768
- Full Text :
- https://doi.org/10.1104/pp.19.01265