The calcium-dependent protein kinase CPK28 negatively regulates the BIK1-mediated PAMP-induced calcium burst

Monaghan, Jacqueline; Matschi, Susanne; Romeis, Tina; Zipfel, Cyril

doi:10.1080/15592324.2015.1018497

Cited by 70 publications

(66 citation statements)

References 30 publications

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“…Here we decipher that in Arabidopsis, three AtMAT proteins are phosphorylated by CPK28. This is consistent with the phosphorylation of BIK1 by CPK28, which favors BIK1 turnover and attenuates pathogen‐associated molecular pattern‐triggered immune responses (Monaghan et al ., , ). Because the effect of CPK28 on BIK1 phosphorylation is essential for plant immune responses, it will be of interest to investigate the role of post‐translational modification of MAT in plant immunity.…”

Section: Discussionmentioning

confidence: 99%

“…Notably, one of the calcium‐dependent protein kinases, AtCPK28, has recently been identified to play a triple role. First, CPK28 lowered BOTRYTIS‐INDUCED KINASE1 (BIK1)‐mediated immune responses by phosphorylating and destabilizing BIK1 in seedlings (Monaghan et al ., , ). Second, CPK28 regulated secondary growth by the balance of jasmonic acid (JA) and GA in its generative phase; cpk28 mutants exhibited growth reduction and ectopic lignifications in stems, following with enhanced expression levels of JA marker genes and reduced expression of a key regulator of GA homeostasis (Matschi et al ., , ).…”

Section: Introductionmentioning

confidence: 99%

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Calcium‐dependent protein kinase CPK28 targets the methionine adenosyltransferases for degradation by the 26S proteasome and affects ethylene biosynthesis and lignin deposition in Arabidopsis

Zhu

et al. 2017

The Plant Journal

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S-adenosylmethionine (AdoMet) is synthesized by methionine adenosyltransferase (MAT), and plays an essential role in ethylene biosynthesis and other methylation reactions. Despite increasing knowledge of MAT regulation at transcriptional levels, how MAT is post-translationally regulated remains unknown in plant cells. Phosphorylation is an important post-translational modification for regulating the activity of enzymes, protein function and signaling transduction. Using molecular and biochemical approaches, we have identified the phosphorylation of MAT proteins by calcium-dependent protein kinase (CPK28). Phenotypically, both MAT2-overexpressing transgenic plants and cpk28 mutants display short hypocotyls and ectopic lignifications. Their shortened hypocotyl phenotypes are caused by ethylene overproduction and rescued by ethylene biosynthesis inhibitor aminoethoxyvinylglycine treatment. Genetic evidence reveals that MAT2 mutation restores the phenotype of ectopic lignification in CPK28-deficient plants. We find that total MAT proteins and AdoMet are increased in cpk28 mutants, but decreased in CPK28-overexpressing seedlings. We also find that MATs in OE::CPK28 are degraded through the 26S proteasome pathway. Our work suggests that CPK28 targets MATs (MAT1, MAT2 and MAT3) for degradation by the 26S proteasome pathway, and thus affects ethylene biosynthesis and lignin deposition in Arabidopsis.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Calcium‐dependent protein kinase CPK28 targets the methionine adenosyltransferases for degradation by the 26S proteasome and affects ethylene biosynthesis and lignin deposition in Arabidopsis

Zhu

et al. 2017

The Plant Journal

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“…Plant protein kinases such as calcium-dependent protein kinases (CDPKs) play central role in mediating plant response to stress signaling3940. The calcium sensor calcineurin B-like proteins (CBLs) and their target kinase CBL-interacting protein kinases (CIPKs) system function together to regulate plant environmental stresses, such as drought10.…”

Section: Discussionmentioning

confidence: 99%

Evolution of an intron-poor cluster of the CIPK gene family and expression in response to drought stress in soybean

Zhu

Chen

Liu

et al. 2016

Sci Rep

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Calcium ion is an intracellular messenger that plays a central role in signal transduction pathways. Calcineurin B-like proteins (CBLs) and CBL-interacting protein kinases (CIPKs) signal network have shown different functions in the Ca2+ signaling process. In this work, we identified the entire soybean (Glycine max) CIPK gene family, which comprised 52 genes and divided into four subgroups (I to IV) based on phylogeny. The gene structural analysis separated these 52 genes into an intron-rich clade and an intron-poor clade. Chromosomal location analysis resulted in the identification of 22 duplicated blocks and six tandem duplication events. Phylogenetic classification of 193 CIPK proteins from representative plant species suggested that the intron-poor clade of CIPKs originated in seed plants. Analysis of global gene expression patterns of soybean CIPK family revealed that most intron-poor soybean CIPK genes are drought-inducible; a finding that was further confirmed using qRT-PCR. Our study provides a foundation for further functional analysis to reveal the roles that CIPKs and more specifically the intron-poor clade play in drought tolerance in soybean.

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“…FLS2 activation disrupts this negative control circuit, resulting in BAK1 phosphorylation and activation of PTI. Furthermore, CALCIUM-DEPENDENT PROTEIN KINASE 28 (CPK28) controls the stability and phosphorylation status of BIK1, an RLCK and important hub in LRR-RK-mediated PTI (Monaghan et al, 2015;Couto et al, 2016;Wang et al, 2018). bir2, pp2A and cpk28 loss-of-function alleles were tested for changes in flg22-or nlp20-induced ROS production.…”

Section: New Phytologistmentioning

confidence: 99%

Comparing Arabidopsis receptor kinase and receptor protein‐mediated immune signaling reveals BIK1‐dependent differences

et al. 2018

Self Cite

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Summary Pattern recognition receptors (PRRs) sense microbial patterns and activate innate immunity against attempted microbial invasions. The leucine‐rich repeat receptor kinases (LRR‐RK) FLS2 and EFR, and the LRR receptor protein (LRR‐RP) receptors RLP23 and RLP42, respectively, represent prototypical members of these two prominent and closely related PRR families. We conducted a survey of Arabidopsis thaliana immune signaling mediated by these receptors to address the question of commonalities and differences between LRR‐RK and LRR‐RP signaling. Quantitative differences in timing and amplitude were observed for several early immune responses, with RP‐mediated responses typically being slower and more prolonged than those mediated by RKs. Activation of RLP23, but not FLS2, induced the production of camalexin. Transcriptomic analysis revealed that RLP23‐regulated genes represent only a fraction of those genes differentially expressed upon FLS2 activation. Several positive and negative regulators of FLS2‐signaling play similar roles in RLP23 signaling. Intriguingly, the cytoplasmic receptor kinase BIK1, a positive regulator of RK signaling, acts as a negative regulator of RP‐type immune receptors in a manner dependent on BIK1 kinase activity. Our study unveiled unexpected differences in two closely related receptor systems and reports a new negative role of BIK1 in plant immunity.

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The calcium-dependent protein kinase CPK28 negatively regulates the BIK1-mediated PAMP-induced calcium burst

Cited by 70 publications

References 30 publications

Calcium‐dependent protein kinase CPK28 targets the methionine adenosyltransferases for degradation by the 26S proteasome and affects ethylene biosynthesis and lignin deposition in Arabidopsis

Calcium‐dependent protein kinase CPK28 targets the methionine adenosyltransferases for degradation by the 26S proteasome and affects ethylene biosynthesis and lignin deposition in Arabidopsis

Evolution of an intron-poor cluster of the CIPK gene family and expression in response to drought stress in soybean

Comparing Arabidopsis receptor kinase and receptor protein‐mediated immune signaling reveals BIK1‐dependent differences

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