PLANT NATRIURETIC PEPTIDE A and Its Putative Receptor PNP-R2 Antagonize Salicylic Acid-Mediated Signaling and Cell Death.
Keun Pyo LeeKaiwei LiuEun Yu KimLaura Medina-PucheHaihong DongJianli DuanMengping LiVivek DograYingrui LiRuiqing LyuZihao LiRenyi LiuChanhong KimPublished in: The Plant cell (2020)
The plant stress hormone salicylic acid (SA) participates in local and systemic acquired resistance, which eventually leads to whole-plant resistance to bacterial pathogens. However, if SA-mediated signaling is not appropriately controlled, plants incur defense-associated fitness costs such as growth inhibition and cell death. Despite its importance, to date only a few components counteracting the SA-primed stress responses have been identified in Arabidopsis (Arabidopsis thaliana). These include other plant hormones such as jasmonic acid and abscisic acid, and proteins such as LESION SIMULATING DISEASE1, a transcription coregulator. Here, we describe PLANT NATRIURETIC PEPTIDE A (PNP-A), a functional analog to vertebrate atrial natriuretic peptides, that appears to antagonize the SA-mediated plant stress responses. While loss of PNP-A potentiates SA-mediated signaling, exogenous application of synthetic PNP-A or overexpression of PNP-A significantly compromises the SA-primed immune responses. Moreover, we identify a plasma membrane-localized receptor-like protein, PNP-R2, that interacts with PNP-A and is required to initiate the PNP-A-mediated intracellular signaling. In summary, our work identifies a peptide and its putative cognate receptor as counteracting both SA-mediated signaling and SA-primed cell death in Arabidopsis.
Keyphrases
- cell death
- immune response
- transcription factor
- cell wall
- arabidopsis thaliana
- physical activity
- gene expression
- cell proliferation
- toll like receptor
- cell cycle arrest
- multidrug resistant
- oxidative stress
- plant growth
- antimicrobial resistance
- heat shock
- inflammatory response
- dendritic cells
- reactive oxygen species
- signaling pathway
- gram negative
- pi k akt
- amino acid