ArticlePlant molecular biology2016
The plant natriuretic peptide receptor is a guanylyl cyclase and enables cGMP-dependent signaling.
Article in Plant molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 51 citations in OpenAlex.
- Small Signaling Peptides inPlant direct · 2026Article
- Guanylate cyclase activity in moss: revisiting the role of ERECTA-like receptors.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- "Cyclic nucleotides in plants: from obscure messengers to central regulators".Frontiers in plant science · 2025Review
- Moonlighting Crypto-Enzymes and Domains as Ancient and Versatile Signaling Devices.International journal of molecular sciences · 2024Review
- Peptide-Mediated Cyclic Nucleotide Signaling in Plants: Identification and Characterization of Interactor Proteins with Nucleotide Cyclase Activity.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Plant adenylate cyclases have come full circle.Nature plants · 2023Review
- A methane-cGMP module positively influences adventitious rooting.Plant cell reports · 2023Article
- HPlant, cell & environment · 2023Review
- Amino acid motifs for the identification of novel protein interactants.Computational and structural biotechnology journal · 2023Review
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- Computational Identification of Functional Centers in Complex Proteins: A Step-by-Step Guide With Examples.Frontiers in bioinformatics · 2021Article
- Arabidopsis Plant Natriuretic Peptide Is a Novel Interactor of Rubisco Activase.Life (Basel, Switzerland) · 2020Article
- A natriuretic peptide from Arabidopsis thaliana (AtPNP-A) can modulate catalase 2 activity.Scientific reports · 2020Article
- PLANT NATRIURETIC PEPTIDE A and Its Putative Receptor PNP-R2 Antagonize Salicylic Acid-Mediated Signaling and Cell Death.The Plant cell · 2020Article
- Dataset on interactors of theData in brief · 2020Article
- Characterization of tomato protein kinases embedding guanylate cyclase catalytic center motif.Scientific reports · 2020Article
- Dual Activities of Plant cGMP-Dependent Protein Kinase and Its Roles in Gibberellin Signaling and Salt Stress.The Plant cell · 2019Article
- Natriuretic peptides appeared after their receptors in vertebrates.BMC evolutionary biology · 2019Article
- Apoplastic invasion patterns triggering plant immunity: plasma membrane sensing at the frontline.Molecular plant pathology · 2019Review
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional homologues of vertebrate natriuretic peptides (NPs), the plant natriuretic peptides (PNPs), are a novel class of peptidic hormones that signal via guanosine 3',5'-cyclic monophosphate (cGMP) and systemically affect plant salt and water balance and responses to biotrophic plant pathogens. Although there is increasing understanding of the complex roles of PNPs in plant responses at the systems level, little is known about the underlying signaling mechanisms. Here we report isolation and identification of a novel Leucine-Rich Repeat (LRR) protein that directly interacts with A. thaliana PNP, AtPNP-A. In vitro binding studies revealed that the Arabidopsis AtPNP-A binds specifically to the LRR protein, termed AtPNP-R1, and the active region of AtPNP-A is sufficient for the interaction to occur. Importantly, the cytosolic part of the AtPNP-R1, much like in some vertebrate NP receptors, harbors a catalytic center diagnostic for guanylyl cyclases and the recombinant AtPNP-R1 is capable of catalyzing the conversion of guanosine triphosphate to cGMP. In addition, we show that AtPNP-A causes rapid increases of cGMP levels in wild type (WT) leaf tissue while this response is significantly reduced in the atpnp-r1 mutants. AtPNP-A also causes cGMP-dependent net water uptake into WT protoplasts, and hence volume increases, whereas responses of the protoplasts from the receptor mutant are impaired. Taken together, our results suggest that the identified LRR protein is an AtPNP-A receptor essential for the PNP-dependent regulation of ion and water homeostasis in plants and that PNP- and vertebrate NP-receptors and their signaling mechanisms share surprising similarities.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.