Phosphorylation of the dimeric cytoplasmic domain of the phytosulfokine receptor, PSKR1

Muleya, Victor; Marondedze, Claudius; Wheeler, Janet; Thomas, Ludivine; Mok, Yee Fong; Griffin, Michael D. W.; Manallack, David T.; Kwezi, Lusisizwe; Lilley, Kathryn S.; Gehring, Chris; Irving, Helen Ruth

doi:10.1042/bcj20160593

Cited by 28 publications

(31 citation statements)

References 61 publications

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“…Whether the reduction in GC activity observed in the BRI1 mutants is due to lack of kinase activity or lack of phosphorylated residues remains to be investigated. A recent study with recombinant cytoplasmic domain of PSKR1 suggests that the phosphorylation status may be more important as mutations to the kinase active site that inhibited kinase activity did not modulate GC activity (Muleya et al ., ).…”

Section: Resultsmentioning

confidence: 97%

“…Indeed phosphorylation status of PSKR1 and/or its kinase activity is important in modulating the ability of the recombinant protein to generate cGMP. Mutations in the juxtamembrane position suppressed GC activity despite alternative effects on kinase activity whereas mutations in the active site that abolished kinase activity had no effect on GC activity (Muleya et al ., ). We transiently expressed GFP‐tagged full‐length wild‐type BRI1, BRI1Y956F and BRI1KR1083/4AA in tobacco.…”

Section: Resultsmentioning

confidence: 97%

“…The superimposed extracted mass chromatograms of m/z 346.06 [M+H] + ion of cGMP all have the corresponding product ion at m/z 152.06 [M+H] + and this confirmed the presence of cGMP in the reaction mixtures of the respective recombinant BRI proteins (Figure b, c). Similar amounts of cGMP are generated by the recombinant cytoplasmic domain and the full‐length PSKR1 (Kwezi et al ., ; Muleya et al ., , ). It is noteworthy that a recently characterized adenylate cyclase from Arabidopsis (AtKUP7) also has activity resembling that of plant GCs (Al‐Younis et al ., ).…”

Section: Resultsmentioning

confidence: 99%

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The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP‐dependent downstream signaling

et al. 2017

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The brassinosteroid receptor brassinosteroid insensitive 1 (BRI1) is a member of the leucine-rich repeat receptor-like kinase family. The intracellular kinase domain of BRI1 is an active kinase and also encapsulates a guanylate cyclase catalytic centre. Using liquid chromatography tandem mass spectrometry, we confirmed that the recombinant cytoplasmic domain of BRI1 generates pmol amounts of cGMP per μg protein with a preference for magnesium over manganese as a co-factor. Importantly, a functional BRI1 kinase is essential for optimal cGMP generation. Therefore, the guanylate cyclase activity of BRI1 is modulated by the kinase while cGMP, the product of the guanylate cyclase, in turn inhibits BRI1 kinase activity. Furthermore, we show using Arabidopsis root cell cultures that cGMP rapidly potentiates phosphorylation of the downstream substrate brassinosteroid signaling kinase 1 (BSK1). Taken together, our results suggest that cGMP acts as a modulator that enhances downstream signaling while dampening signal generation from the receptor.

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

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The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP‐dependent downstream signaling

et al. 2017

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“…4,7 One of the missing components may be phosphorylation of specific residues in the kinase domain as certain phosphorylated residues are necessary for GC activity of PSKR1 and BRI1. 7,11 Interestingly, some of these residues also contribute to the kinase activity. [11][12][13][14] Thus phosphorylation status is a component necessary for activation of both the kinase and GC elements of the receptor kinases BRI1 and PSKR1.…”

Section: Introductionmentioning

confidence: 99%

“…7,11 Interestingly, some of these residues also contribute to the kinase activity. [11][12][13][14] Thus phosphorylation status is a component necessary for activation of both the kinase and GC elements of the receptor kinases BRI1 and PSKR1. 7,[11][12][13][14][15] Both BRI1 and PSKR1 are dual tyrosine and serine/threonine kinases.…”

Section: Introductionmentioning

confidence: 99%

Intramolecular crosstalk between catalytic activities of receptor kinases

Kwezi

Wheeler

Marondedze

et al. 2018

Plant Signaling & Behavior

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Signal modulation is important for the growth and development of plants and this process is mediated by a number of factors including physiological growth regulators and their associated signal transduction pathways. Protein kinases play a central role in signaling, including those involving pathogen response mechanisms. We previously demonstrated an active guanylate cyclase (GC) catalytic center in the brassinosteroid insensitive receptor (AtBRI1) within an active intracellular kinase domain resulting in dual enzymatic activity. Here we propose a novel type of receptor architecture that is characterized by a functional GC catalytic center nested in the cytosolic kinase domain enabling intramolecular crosstalk. This may be through a cGMP-AtBRI1 complex forming that may induce a negative feedback mechanism leading to desensitisation of the receptor, regulated through the cGMP production pathway. We further argue that the comparatively low but highly localized cGMP generated by the GC in response to a ligand is sufficient to modulate the kinase activity. This type of receptor therefore provides a molecular switch that directly and/or indirectly affects ligand dependent phosphorylation of downstream signaling cascades and suggests that subsequent signal transduction and modulation works in conjunction with the kinase in downstream signaling.

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Plant Natriuretic Peptides

Gehring¹

2019

Encyclopedia of Life Sciences

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Plant natriuretic peptides (PNPs) belong to a growing number of plant peptide hormones. PNPs were first immuno‐affinity purified from ivy with an antibody against the vertebrate atrial natriuretic peptide (ANP) and were shown to affect a number of physiological responses, including stomatal movements and abiotic and biotic stress responses. PNPs are secreted into the apoplastic space and are systemically mobile. They act at nanomolar concentrations and in a 3′,5′‐cyclic guanosine monophosphate (cGMP)‐dependent manner. The Arabidopsis thaliana PNP (AtPNP‐A) is distantly related to expansins, but it does not contain a wall‐binding domain consistent with its systemic mode of action. The first AtPNP‐A receptor (AtPNP‐R1) is a novel leucine‐rich repeat receptor kinase located in the cell membrane and harbours a functional guanylyl cyclase in the cytosolic part essential for cGMP‐dependent responses. Finally, PNPs have also been acquired by several plant pathogens through ancient horizontal gene transfer and interfere with host defences to the detriment of their hosts. Key Concepts Most currently established plant hormones are small molecules that can act on the site of synthesis or at a distance from their site of synthesis, within or between plants. Plant peptide hormones are a new and rapidly expanding class of plant hormones that have important roles in growth, development and responses to the environment and in particular the defence against pathogens. Plant peptide hormones, including plant natriuretic peptides (PNPs), are systemically mobile and can signal through membrane‐associated receptor kinases some of which harbour functional guanylyl cyclase catalytic centres capable of converting GTP to cGMP. cGMP, in turn, is a key messenger in plant responses to the environment that enables and modulates downstream responses including cGMP‐dependent protein phosphorylation and the activation of cyclic nucleotide‐gated channels (CNGCs). Animal natriuretic peptides (ANPs), although not orthologs of PNPs, can trigger similar responses in plants, and both can act as ligands for their membrane‐associated receptors that harbour guanylyl cyclases capable of generating cGMP from GTP. PNPs have been acquired by some plant pathogens through ancient horizontal gene transfer (HGT). These pathogens make use of the plant peptide hormones to interfere with host defences to their advantage and the detriment of the host. The use of horizontally acquired PNPs in plant pathogens can afford new insights into host‐pathogen biology and may inform novel approaches to pest control.

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Phosphorylation of the dimeric cytoplasmic domain of the phytosulfokine receptor, PSKR1

Cited by 28 publications

References 61 publications

The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP‐dependent downstream signaling

The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP‐dependent downstream signaling

Intramolecular crosstalk between catalytic activities of receptor kinases

Plant Natriuretic Peptides

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