The plant natriuretic peptide receptor is a guanylyl cyclase and enables cGMP-dependent signaling
Type
ArticleAuthors
Turek, Ilona
Gehring, Christoph A

KAUST Department
Biological and Environmental Sciences and Engineering (BESE) DivisionBioscience Program
Chemical and Biological Engineering Program
Date
2016-03-05Online Publication Date
2016-03-05Print Publication Date
2016-06Permanent link to this record
http://hdl.handle.net/10754/621442
Metadata
Show full item recordAbstract
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. © 2016 Springer Science+Business Media DordrechtCitation
Turek I, Gehring C (2016) The plant natriuretic peptide receptor is a guanylyl cyclase and enables cGMP-dependent signaling. Plant Molecular Biology 91: 275–286. Available: http://dx.doi.org/10.1007/s11103-016-0465-8.Sponsors
King Abdullah University of Science and TechnologyPublisher
Springer NatureJournal
Plant Molecular BiologyPubMed ID
26945740ae974a485f413a2113503eed53cd6c53
10.1007/s11103-016-0465-8