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      The Complex Story of Plant Cyclic Nucleotide-Gated Channels

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          Abstract

          Plant cyclic nucleotide-gated channels (CNGCs) are tetrameric cation channels which may be activated by the cyclic nucleotides (cNMPs) adenosine 3′,5′-cyclic monophosphate (cAMP) and guanosine 3′,5′-cyclic monophosphate (cGMP). The genome of Arabidopsis thaliana encodes 20 CNGC subunits associated with aspects of development, stress response and immunity. Recently, it has been demonstrated that CNGC subunits form heterotetrameric complexes which behave differently from the homotetramers produced by their constituent subunits. These findings have widespread implications for future signalling research and may help explain how specificity can be achieved by CNGCs that are known to act in disparate pathways. Regulation of complex formation may involve cyclic nucleotide-gated channel-like proteins.

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          Most cited references138

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          A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity.

          Plants and animals rely on innate immunity to prevent infections by detection of microbe-associated molecular patterns (MAMPs) through pattern-recognition receptors (PRRs). The plant PRR FLS2, a leucine-rich repeat-receptor kinase, recognizes bacterial flagellin and initiates immune signaling by association with another leucine-rich repeat-receptor-like kinase, BAK1. It remains unknown how the FLS2/BAK1 receptor complex activates intracellular signaling cascades. Here we identified the receptor-like cytoplasmic kinase BIK1 that is rapidly phosphorylated upon flagellin perception, depending on both FLS2 and BAK1. BIK1 associates with FLS2 and BAK1 in vivo and in vitro. BIK1 is phosphorylated by BAK1, and BIK1 also directly phosphorylates BAK1 and FLS2 in vitro. The flagellin phosphorylation site Thr(237) of BIK1 is required for its phosphorylation on BAK1 and FLS2, suggesting that BIK1 is likely first phosphorylated upon flagellin perception and subsequently transphosphorylates FLS2/BAK1 to propagate flagellin signaling. Importantly, bik1 mutants are compromised in diverse flagellin-mediated responses and immunity to the nonpathogenic bacterial infection. Thus, BIK1 is an essential component in MAMP signal transduction, which links the MAMP receptor complex to downstream intracellular signaling.
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            FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis.

            Flagellin, the main protein of the bacterial flagella, elicits defence responses and alters growth in Arabidopsis seedlings. Previously, we identified the FLS1 locus, which confers flagellin insensitivity in Ws-0. To identify additional components involved in flagellin perception, we screened for flagellin insensitivity mutants in the flagellin-sensitive accession La-er. Here, we describe the identification of a new locus, FLS2, by a map-based strategy. The FLS2 gene is ubiquitously expressed and encodes a putative receptor kinase. FLS2 shares structural and functional homologies with known plant resistance genes and with components involved in the innate immune system of mammals and insects.
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              A calmodulin-gated calcium channel links pathogen patterns to plant immunity

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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                16 January 2021
                January 2021
                : 22
                : 2
                : 874
                Affiliations
                Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, UK; ecj39@ 123456cam.ac.uk (E.J.-B.); lw577@ 123456cam.ac.uk (L.W.); yn283@ 123456cam.ac.uk (Y.N.)
                Author notes
                [* ]Correspondence: jmd32@ 123456cam.ac.uk ; Tel.: +44-1223-333-939
                Author information
                https://orcid.org/0000-0003-2018-3441
                Article
                ijms-22-00874
                10.3390/ijms22020874
                7830781
                33467208
                c970fb22-3356-48ee-a0c3-ae2d24337a32
                © 2021 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 11 December 2020
                : 15 January 2021
                Categories
                Review

                Molecular biology
                calcium signalling,cam,calmodulin,camp,cgmp,cngc,cyclic nucleotide-gated channel,cngcl,cyclic nucleotide-gated channel like

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